data_5B22 # _entry.id 5B22 # _audit_conform.dict_name mmcif_pdbx.dic _audit_conform.dict_version 5.279 _audit_conform.dict_location http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic # loop_ _database_2.database_id _database_2.database_code PDB 5B22 WWPDB D_1300000008 # _pdbx_database_related.db_name PDB _pdbx_database_related.details . _pdbx_database_related.db_id 5B21 _pdbx_database_related.content_type unspecified # _pdbx_database_status.status_code REL _pdbx_database_status.status_code_sf REL _pdbx_database_status.status_code_mr ? _pdbx_database_status.entry_id 5B22 _pdbx_database_status.recvd_initial_deposition_date 2015-12-28 _pdbx_database_status.SG_entry N _pdbx_database_status.deposit_site PDBJ _pdbx_database_status.process_site PDBJ _pdbx_database_status.status_code_cs ? _pdbx_database_status.methods_development_category ? _pdbx_database_status.pdb_format_compatible Y # loop_ _audit_author.name _audit_author.pdbx_ordinal 'Takebe, K.' 1 'Sangawa, T.' 2 'Katsutani, T.' 3 'Narita, H.' 4 'Suzuki, M.' 5 # _citation.abstract ? _citation.abstract_id_CAS ? _citation.book_id_ISBN ? _citation.book_publisher ? _citation.book_publisher_city ? _citation.book_title ? _citation.coordinate_linkage ? _citation.country ? _citation.database_id_Medline ? _citation.details ? _citation.id primary _citation.journal_abbrev 'To Be Published' _citation.journal_id_ASTM ? _citation.journal_id_CSD 0353 _citation.journal_id_ISSN ? _citation.journal_full ? _citation.journal_issue ? _citation.journal_volume ? _citation.language ? _citation.page_first ? _citation.page_last ? _citation.title 'Dimer structure of murine Nectin-3 D1D2' _citation.year ? _citation.database_id_CSD ? _citation.pdbx_database_id_DOI ? _citation.pdbx_database_id_PubMed ? _citation.unpublished_flag ? # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Sangawa, T.' 1 primary 'Takebe, K.' 2 primary 'Katsutani, T.' 3 primary 'Narita, H.' 4 primary 'Suzuki, M.' 5 # _cell.entry_id 5B22 _cell.length_a 151.650 _cell.length_b 72.880 _cell.length_c 81.930 _cell.angle_alpha 90.00 _cell.angle_beta 116.36 _cell.angle_gamma 90.00 _cell.Z_PDB 8 _cell.pdbx_unique_axis ? # _symmetry.entry_id 5B22 _symmetry.space_group_name_H-M 'C 1 2 1' _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.cell_setting ? _symmetry.Int_Tables_number 5 # loop_ _entity.id _entity.type _entity.src_method _entity.pdbx_description _entity.formula_weight _entity.pdbx_number_of_molecules _entity.pdbx_ec _entity.pdbx_mutation _entity.pdbx_fragment _entity.details 1 polymer man Nectin-3 23127.213 2 ? ? 'UNP residues 59-266' ? 2 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 4 ? ? ? ? 3 non-polymer man BETA-D-MANNOSE 180.156 2 ? ? ? ? 4 water nat water 18.015 183 ? ? ? ? # _entity_name_com.entity_id 1 _entity_name_com.name 'Nectin cell adhesion molecule 3,Poliovirus receptor-related protein 3' # _entity_poly.entity_id 1 _entity_poly.type 'polypeptide(L)' _entity_poly.nstd_linkage no _entity_poly.nstd_monomer no _entity_poly.pdbx_seq_one_letter_code ;PSIIVEPHVTAVWGKNVSLKCLIEVNETITQISWEKIHGKSTQTVAVHHPQYGFSVQGDYQGRVLFKNYSLNDATITLHN IGFSDSGKYICKAVTFPLGNAQSSTTVTVLVEPTVSLIKGPDSLIDGGNETVAAVCVAATGKPVAQIDWEGDLGEMESST TSFPNETATIVSQYKLFPTRFARGRRITCVVKHPALEKDIRYSFILDIQHH ; _entity_poly.pdbx_seq_one_letter_code_can ;PSIIVEPHVTAVWGKNVSLKCLIEVNETITQISWEKIHGKSTQTVAVHHPQYGFSVQGDYQGRVLFKNYSLNDATITLHN IGFSDSGKYICKAVTFPLGNAQSSTTVTVLVEPTVSLIKGPDSLIDGGNETVAAVCVAATGKPVAQIDWEGDLGEMESST TSFPNETATIVSQYKLFPTRFARGRRITCVVKHPALEKDIRYSFILDIQHH ; _entity_poly.pdbx_strand_id A,B _entity_poly.pdbx_target_identifier ? # loop_ _entity_poly_seq.entity_id _entity_poly_seq.num _entity_poly_seq.mon_id _entity_poly_seq.hetero 1 1 PRO n 1 2 SER n 1 3 ILE n 1 4 ILE n 1 5 VAL n 1 6 GLU n 1 7 PRO n 1 8 HIS n 1 9 VAL n 1 10 THR n 1 11 ALA n 1 12 VAL n 1 13 TRP n 1 14 GLY n 1 15 LYS n 1 16 ASN n 1 17 VAL n 1 18 SER n 1 19 LEU n 1 20 LYS n 1 21 CYS n 1 22 LEU n 1 23 ILE n 1 24 GLU n 1 25 VAL n 1 26 ASN n 1 27 GLU n 1 28 THR n 1 29 ILE n 1 30 THR n 1 31 GLN n 1 32 ILE n 1 33 SER n 1 34 TRP n 1 35 GLU n 1 36 LYS n 1 37 ILE n 1 38 HIS n 1 39 GLY n 1 40 LYS n 1 41 SER n 1 42 THR n 1 43 GLN n 1 44 THR n 1 45 VAL n 1 46 ALA n 1 47 VAL n 1 48 HIS n 1 49 HIS n 1 50 PRO n 1 51 GLN n 1 52 TYR n 1 53 GLY n 1 54 PHE n 1 55 SER n 1 56 VAL n 1 57 GLN n 1 58 GLY n 1 59 ASP n 1 60 TYR n 1 61 GLN n 1 62 GLY n 1 63 ARG n 1 64 VAL n 1 65 LEU n 1 66 PHE n 1 67 LYS n 1 68 ASN n 1 69 TYR n 1 70 SER n 1 71 LEU n 1 72 ASN n 1 73 ASP n 1 74 ALA n 1 75 THR n 1 76 ILE n 1 77 THR n 1 78 LEU n 1 79 HIS n 1 80 ASN n 1 81 ILE n 1 82 GLY n 1 83 PHE n 1 84 SER n 1 85 ASP n 1 86 SER n 1 87 GLY n 1 88 LYS n 1 89 TYR n 1 90 ILE n 1 91 CYS n 1 92 LYS n 1 93 ALA n 1 94 VAL n 1 95 THR n 1 96 PHE n 1 97 PRO n 1 98 LEU n 1 99 GLY n 1 100 ASN n 1 101 ALA n 1 102 GLN n 1 103 SER n 1 104 SER n 1 105 THR n 1 106 THR n 1 107 VAL n 1 108 THR n 1 109 VAL n 1 110 LEU n 1 111 VAL n 1 112 GLU n 1 113 PRO n 1 114 THR n 1 115 VAL n 1 116 SER n 1 117 LEU n 1 118 ILE n 1 119 LYS n 1 120 GLY n 1 121 PRO n 1 122 ASP n 1 123 SER n 1 124 LEU n 1 125 ILE n 1 126 ASP n 1 127 GLY n 1 128 GLY n 1 129 ASN n 1 130 GLU n 1 131 THR n 1 132 VAL n 1 133 ALA n 1 134 ALA n 1 135 VAL n 1 136 CYS n 1 137 VAL n 1 138 ALA n 1 139 ALA n 1 140 THR n 1 141 GLY n 1 142 LYS n 1 143 PRO n 1 144 VAL n 1 145 ALA n 1 146 GLN n 1 147 ILE n 1 148 ASP n 1 149 TRP n 1 150 GLU n 1 151 GLY n 1 152 ASP n 1 153 LEU n 1 154 GLY n 1 155 GLU n 1 156 MET n 1 157 GLU n 1 158 SER n 1 159 SER n 1 160 THR n 1 161 THR n 1 162 SER n 1 163 PHE n 1 164 PRO n 1 165 ASN n 1 166 GLU n 1 167 THR n 1 168 ALA n 1 169 THR n 1 170 ILE n 1 171 VAL n 1 172 SER n 1 173 GLN n 1 174 TYR n 1 175 LYS n 1 176 LEU n 1 177 PHE n 1 178 PRO n 1 179 THR n 1 180 ARG n 1 181 PHE n 1 182 ALA n 1 183 ARG n 1 184 GLY n 1 185 ARG n 1 186 ARG n 1 187 ILE n 1 188 THR n 1 189 CYS n 1 190 VAL n 1 191 VAL n 1 192 LYS n 1 193 HIS n 1 194 PRO n 1 195 ALA n 1 196 LEU n 1 197 GLU n 1 198 LYS n 1 199 ASP n 1 200 ILE n 1 201 ARG n 1 202 TYR n 1 203 SER n 1 204 PHE n 1 205 ILE n 1 206 LEU n 1 207 ASP n 1 208 ILE n 1 209 GLN n 1 210 HIS n 1 211 HIS n # _entity_src_gen.entity_id 1 _entity_src_gen.pdbx_src_id 1 _entity_src_gen.pdbx_alt_source_flag sample _entity_src_gen.pdbx_seq_type 'Biological sequence' _entity_src_gen.pdbx_beg_seq_num 1 _entity_src_gen.pdbx_end_seq_num 211 _entity_src_gen.gene_src_common_name Mouse _entity_src_gen.gene_src_genus ? _entity_src_gen.pdbx_gene_src_gene 'Nectin3, Pvrl3' _entity_src_gen.gene_src_species ? _entity_src_gen.gene_src_strain ? _entity_src_gen.gene_src_tissue ? _entity_src_gen.gene_src_tissue_fraction ? _entity_src_gen.gene_src_details ? _entity_src_gen.pdbx_gene_src_fragment ? _entity_src_gen.pdbx_gene_src_scientific_name 'Mus musculus' _entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 10090 _entity_src_gen.pdbx_gene_src_variant ? _entity_src_gen.pdbx_gene_src_cell_line ? _entity_src_gen.pdbx_gene_src_atcc ? _entity_src_gen.pdbx_gene_src_organ ? _entity_src_gen.pdbx_gene_src_organelle ? _entity_src_gen.pdbx_gene_src_cell ? _entity_src_gen.pdbx_gene_src_cellular_location ? _entity_src_gen.host_org_common_name ? _entity_src_gen.pdbx_host_org_scientific_name 'Spodoptera frugiperda' _entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 7108 _entity_src_gen.host_org_genus ? _entity_src_gen.pdbx_host_org_gene ? _entity_src_gen.pdbx_host_org_organ ovary _entity_src_gen.host_org_species ? _entity_src_gen.pdbx_host_org_tissue ? _entity_src_gen.pdbx_host_org_tissue_fraction ? _entity_src_gen.pdbx_host_org_strain ? _entity_src_gen.pdbx_host_org_variant ? _entity_src_gen.pdbx_host_org_cell_line Sf-9 _entity_src_gen.pdbx_host_org_atcc ? _entity_src_gen.pdbx_host_org_culture_collection ? _entity_src_gen.pdbx_host_org_cell ? _entity_src_gen.pdbx_host_org_organelle ? _entity_src_gen.pdbx_host_org_cellular_location ? _entity_src_gen.pdbx_host_org_vector_type baculovirus _entity_src_gen.pdbx_host_org_vector ? _entity_src_gen.host_org_details ? _entity_src_gen.expression_system_id ? _entity_src_gen.plasmid_name pFastBac-1 _entity_src_gen.plasmid_details ? _entity_src_gen.pdbx_description ? # _struct_ref.id 1 _struct_ref.db_name UNP _struct_ref.db_code NECT3_MOUSE _struct_ref.pdbx_db_accession Q9JLB9 _struct_ref.pdbx_db_isoform ? _struct_ref.entity_id 1 _struct_ref.pdbx_seq_one_letter_code ;SIIVEPHVTAVWGKNVSLKCLIEVNETITQISWEKIHGKSTQTVAVHHPQYGFSVQGDYQGRVLFKNYSLNDATITLHNI GFSDSGKYICKAVTFPLGNAQSSTTVTVLVEPTVSLIKGPDSLIDGGNETVAAVCVAATGKPVAQIDWEGDLGEMESSTT SFPNETATIVSQYKLFPTRFARGRRITCVVKHPALEKDIRYSFILDIQ ; _struct_ref.pdbx_align_begin 59 # loop_ _struct_ref_seq.align_id _struct_ref_seq.ref_id _struct_ref_seq.pdbx_PDB_id_code _struct_ref_seq.pdbx_strand_id _struct_ref_seq.seq_align_beg _struct_ref_seq.pdbx_seq_align_beg_ins_code _struct_ref_seq.seq_align_end _struct_ref_seq.pdbx_seq_align_end_ins_code _struct_ref_seq.pdbx_db_accession _struct_ref_seq.db_align_beg _struct_ref_seq.pdbx_db_align_beg_ins_code _struct_ref_seq.db_align_end _struct_ref_seq.pdbx_db_align_end_ins_code _struct_ref_seq.pdbx_auth_seq_align_beg _struct_ref_seq.pdbx_auth_seq_align_end 1 1 5B22 A 2 ? 209 ? Q9JLB9 59 ? 266 ? 1 208 2 1 5B22 B 2 ? 209 ? Q9JLB9 59 ? 266 ? 1 208 # loop_ _struct_ref_seq_dif.align_id _struct_ref_seq_dif.pdbx_pdb_id_code _struct_ref_seq_dif.mon_id _struct_ref_seq_dif.pdbx_pdb_strand_id _struct_ref_seq_dif.seq_num _struct_ref_seq_dif.pdbx_pdb_ins_code _struct_ref_seq_dif.pdbx_seq_db_name _struct_ref_seq_dif.pdbx_seq_db_accession_code _struct_ref_seq_dif.db_mon_id _struct_ref_seq_dif.pdbx_seq_db_seq_num _struct_ref_seq_dif.details _struct_ref_seq_dif.pdbx_auth_seq_num _struct_ref_seq_dif.pdbx_ordinal 1 5B22 PRO A 1 ? UNP Q9JLB9 ? ? 'expression tag' 0 1 1 5B22 HIS A 210 ? UNP Q9JLB9 ? ? 'expression tag' 209 2 1 5B22 HIS A 211 ? UNP Q9JLB9 ? ? 'expression tag' 210 3 2 5B22 PRO B 1 ? UNP Q9JLB9 ? ? 'expression tag' 0 4 2 5B22 HIS B 210 ? UNP Q9JLB9 ? ? 'expression tag' 209 5 2 5B22 HIS B 211 ? UNP Q9JLB9 ? ? 'expression tag' 210 6 # loop_ _chem_comp.id _chem_comp.type _chem_comp.mon_nstd_flag _chem_comp.name _chem_comp.pdbx_synonyms _chem_comp.formula _chem_comp.formula_weight ALA 'L-peptide linking' y ALANINE ? 'C3 H7 N O2' 89.093 ARG 'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1' 175.209 ASN 'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3' 132.118 ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4' 133.103 BMA D-saccharide . BETA-D-MANNOSE ? 'C6 H12 O6' 180.156 CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S' 121.158 GLN 'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3' 146.144 GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4' 147.129 GLY 'peptide linking' y GLYCINE ? 'C2 H5 N O2' 75.067 HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 HOH non-polymer . WATER ? 'H2 O' 18.015 ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2' 131.173 LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2' 131.173 LYS 'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1' 147.195 MET 'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S' 149.211 NAG D-saccharide . N-ACETYL-D-GLUCOSAMINE ? 'C8 H15 N O6' 221.208 PHE 'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2' 165.189 PRO 'L-peptide linking' y PROLINE ? 'C5 H9 N O2' 115.130 SER 'L-peptide linking' y SERINE ? 'C3 H7 N O3' 105.093 THR 'L-peptide linking' y THREONINE ? 'C4 H9 N O3' 119.119 TRP 'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2' 204.225 TYR 'L-peptide linking' y TYROSINE ? 'C9 H11 N O3' 181.189 VAL 'L-peptide linking' y VALINE ? 'C5 H11 N O2' 117.146 # _exptl.absorpt_coefficient_mu ? _exptl.absorpt_correction_T_max ? _exptl.absorpt_correction_T_min ? _exptl.absorpt_correction_type ? _exptl.absorpt_process_details ? _exptl.entry_id 5B22 _exptl.crystals_number 1 _exptl.details ? _exptl.method 'X-RAY DIFFRACTION' _exptl.method_details ? # _exptl_crystal.colour ? _exptl_crystal.density_diffrn ? _exptl_crystal.density_Matthews 4.39 _exptl_crystal.density_method ? _exptl_crystal.density_percent_sol 71.95 _exptl_crystal.description ? _exptl_crystal.F_000 ? _exptl_crystal.id 1 _exptl_crystal.preparation ? _exptl_crystal.size_max ? _exptl_crystal.size_mid ? _exptl_crystal.size_min ? _exptl_crystal.size_rad ? _exptl_crystal.colour_lustre ? _exptl_crystal.colour_modifier ? _exptl_crystal.colour_primary ? _exptl_crystal.density_meas ? _exptl_crystal.density_meas_esd ? _exptl_crystal.density_meas_gt ? _exptl_crystal.density_meas_lt ? _exptl_crystal.density_meas_temp ? _exptl_crystal.density_meas_temp_esd ? _exptl_crystal.density_meas_temp_gt ? _exptl_crystal.density_meas_temp_lt ? _exptl_crystal.pdbx_crystal_image_url ? _exptl_crystal.pdbx_crystal_image_format ? _exptl_crystal.pdbx_mosaicity ? _exptl_crystal.pdbx_mosaicity_esd ? # _exptl_crystal_grow.apparatus ? _exptl_crystal_grow.atmosphere ? _exptl_crystal_grow.crystal_id 1 _exptl_crystal_grow.details ? _exptl_crystal_grow.method 'VAPOR DIFFUSION, HANGING DROP' _exptl_crystal_grow.method_ref ? _exptl_crystal_grow.pH ? _exptl_crystal_grow.pressure ? _exptl_crystal_grow.pressure_esd ? _exptl_crystal_grow.seeding ? _exptl_crystal_grow.seeding_ref ? _exptl_crystal_grow.temp 293.15 _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.temp_esd ? _exptl_crystal_grow.time ? _exptl_crystal_grow.pdbx_details '22% PEG 3350, 100mM Imidazole pH7.0, 100mM Ammmonium citrate tribasic' _exptl_crystal_grow.pdbx_pH_range 7.0-7.5 # _diffrn.ambient_environment ? _diffrn.ambient_temp 100 _diffrn.ambient_temp_details ? _diffrn.ambient_temp_esd ? _diffrn.crystal_id 1 _diffrn.crystal_support ? _diffrn.crystal_treatment ? _diffrn.details ? _diffrn.id 1 _diffrn.ambient_pressure ? _diffrn.ambient_pressure_esd ? _diffrn.ambient_pressure_gt ? _diffrn.ambient_pressure_lt ? _diffrn.ambient_temp_gt ? _diffrn.ambient_temp_lt ? # _diffrn_detector.details ? _diffrn_detector.detector PIXEL _diffrn_detector.diffrn_id 1 _diffrn_detector.type 'DECTRIS PILATUS 2M-F' _diffrn_detector.area_resol_mean ? _diffrn_detector.dtime ? _diffrn_detector.pdbx_frames_total ? _diffrn_detector.pdbx_collection_time_total ? _diffrn_detector.pdbx_collection_date 2013-10-23 # _diffrn_radiation.collimation ? _diffrn_radiation.diffrn_id 1 _diffrn_radiation.filter_edge ? _diffrn_radiation.inhomogeneity ? _diffrn_radiation.monochromator ? _diffrn_radiation.polarisn_norm ? _diffrn_radiation.polarisn_ratio ? _diffrn_radiation.probe ? _diffrn_radiation.type ? _diffrn_radiation.xray_symbol ? _diffrn_radiation.wavelength_id 1 _diffrn_radiation.pdbx_monochromatic_or_laue_m_l M _diffrn_radiation.pdbx_wavelength_list ? _diffrn_radiation.pdbx_wavelength ? _diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH' _diffrn_radiation.pdbx_analyzer ? _diffrn_radiation.pdbx_scattering_type x-ray # _diffrn_radiation_wavelength.id 1 _diffrn_radiation_wavelength.wavelength 1.1000 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.current ? _diffrn_source.details ? _diffrn_source.diffrn_id 1 _diffrn_source.power ? _diffrn_source.size ? _diffrn_source.source SYNCHROTRON _diffrn_source.target ? _diffrn_source.type 'PHOTON FACTORY BEAMLINE BL-1A' _diffrn_source.voltage ? _diffrn_source.take-off_angle ? _diffrn_source.pdbx_wavelength_list 1.1000 _diffrn_source.pdbx_wavelength ? _diffrn_source.pdbx_synchrotron_beamline BL-1A _diffrn_source.pdbx_synchrotron_site 'Photon Factory' # _reflns.B_iso_Wilson_estimate ? _reflns.entry_id 5B22 _reflns.data_reduction_details ? _reflns.data_reduction_method ? _reflns.d_resolution_high 2.58 _reflns.d_resolution_low 50.0 _reflns.details ? _reflns.limit_h_max ? _reflns.limit_h_min ? _reflns.limit_k_max ? _reflns.limit_k_min ? _reflns.limit_l_max ? _reflns.limit_l_min ? _reflns.number_all ? _reflns.number_obs 25302 _reflns.observed_criterion ? _reflns.observed_criterion_F_max ? _reflns.observed_criterion_F_min ? _reflns.observed_criterion_I_max ? _reflns.observed_criterion_I_min ? _reflns.observed_criterion_sigma_F ? _reflns.observed_criterion_sigma_I ? _reflns.percent_possible_obs 99.7 _reflns.R_free_details ? _reflns.Rmerge_F_all ? _reflns.Rmerge_F_obs ? _reflns.Friedel_coverage ? _reflns.number_gt ? _reflns.threshold_expression ? _reflns.pdbx_redundancy 2.9 _reflns.pdbx_Rmerge_I_obs 0.11 _reflns.pdbx_Rmerge_I_all ? _reflns.pdbx_Rsym_value ? _reflns.pdbx_netI_over_av_sigmaI ? _reflns.pdbx_netI_over_sigmaI 6.5 _reflns.pdbx_res_netI_over_av_sigmaI_2 ? _reflns.pdbx_res_netI_over_sigmaI_2 ? _reflns.pdbx_chi_squared ? _reflns.pdbx_scaling_rejects ? _reflns.pdbx_d_res_high_opt ? _reflns.pdbx_d_res_low_opt ? _reflns.pdbx_d_res_opt_method ? _reflns.phase_calculation_details ? _reflns.pdbx_Rrim_I_all ? _reflns.pdbx_Rpim_I_all ? _reflns.pdbx_d_opt ? _reflns.pdbx_number_measured_all ? _reflns.pdbx_diffrn_id 1 _reflns.pdbx_ordinal 1 _reflns.pdbx_CC_half ? _reflns.pdbx_R_split ? # _reflns_shell.d_res_high 2.58 _reflns_shell.d_res_low ? _reflns_shell.meanI_over_sigI_all ? _reflns_shell.meanI_over_sigI_obs ? _reflns_shell.number_measured_all ? _reflns_shell.number_measured_obs ? _reflns_shell.number_possible ? _reflns_shell.number_unique_all ? _reflns_shell.number_unique_obs ? _reflns_shell.percent_possible_all 99.8 _reflns_shell.percent_possible_obs ? _reflns_shell.Rmerge_F_all ? _reflns_shell.Rmerge_F_obs ? _reflns_shell.Rmerge_I_all ? _reflns_shell.Rmerge_I_obs ? _reflns_shell.meanI_over_sigI_gt ? _reflns_shell.meanI_over_uI_all ? _reflns_shell.meanI_over_uI_gt ? _reflns_shell.number_measured_gt ? _reflns_shell.number_unique_gt ? _reflns_shell.percent_possible_gt ? _reflns_shell.Rmerge_F_gt ? _reflns_shell.Rmerge_I_gt ? _reflns_shell.pdbx_redundancy 3.1 _reflns_shell.pdbx_Rsym_value ? _reflns_shell.pdbx_chi_squared ? _reflns_shell.pdbx_netI_over_sigmaI_all ? _reflns_shell.pdbx_netI_over_sigmaI_obs ? _reflns_shell.pdbx_Rrim_I_all ? _reflns_shell.pdbx_Rpim_I_all ? _reflns_shell.pdbx_rejects ? _reflns_shell.pdbx_ordinal 1 _reflns_shell.pdbx_diffrn_id 1 _reflns_shell.pdbx_CC_half ? _reflns_shell.pdbx_R_split ? # _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.entry_id 5B22 _refine.pdbx_diffrn_id 1 _refine.pdbx_TLS_residual_ADP_flag ? _refine.ls_number_reflns_obs 25289 _refine.ls_number_reflns_all ? _refine.pdbx_ls_sigma_I ? _refine.pdbx_ls_sigma_F 1.34 _refine.pdbx_data_cutoff_high_absF ? _refine.pdbx_data_cutoff_low_absF ? _refine.pdbx_data_cutoff_high_rms_absF ? _refine.ls_d_res_low 29.770 _refine.ls_d_res_high 2.580 _refine.ls_percent_reflns_obs 99.63 _refine.ls_R_factor_obs 0.2321 _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.2291 _refine.ls_R_factor_R_free 0.2884 _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.ls_percent_reflns_R_free 5.05 _refine.ls_number_reflns_R_free 1277 _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min ? _refine.occupancy_max ? _refine.correlation_coeff_Fo_to_Fc ? _refine.correlation_coeff_Fo_to_Fc_free ? _refine.B_iso_mean ? _refine.aniso_B[1][1] ? _refine.aniso_B[2][2] ? _refine.aniso_B[3][3] ? _refine.aniso_B[1][2] ? _refine.aniso_B[1][3] ? _refine.aniso_B[2][3] ? _refine.solvent_model_details 'FLAT BULK SOLVENT MODEL' _refine.solvent_model_param_ksol ? _refine.solvent_model_param_bsol ? _refine.pdbx_solvent_vdw_probe_radii 1.11 _refine.pdbx_solvent_ion_probe_radii ? _refine.pdbx_solvent_shrinkage_radii 0.90 _refine.pdbx_ls_cross_valid_method 'FREE R-VALUE' _refine.details ? _refine.pdbx_starting_model 4FOM _refine.pdbx_method_to_determine_struct 'MOLECULAR REPLACEMENT' _refine.pdbx_isotropic_thermal_model ? _refine.pdbx_stereochemistry_target_values ML _refine.pdbx_stereochem_target_val_spec_case ? _refine.pdbx_R_Free_selection_details ? _refine.pdbx_overall_ESU_R ? _refine.pdbx_overall_ESU_R_Free ? _refine.overall_SU_ML 0.38 _refine.pdbx_overall_phase_error 29.34 _refine.overall_SU_B ? _refine.overall_SU_R_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_free_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_Blow_DPI ? _refine.pdbx_overall_SU_R_free_Blow_DPI ? # _refine_hist.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_hist.cycle_id LAST _refine_hist.pdbx_number_atoms_protein 3232 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 78 _refine_hist.number_atoms_solvent 183 _refine_hist.number_atoms_total 3493 _refine_hist.d_res_high 2.580 _refine_hist.d_res_low 29.770 # loop_ _refine_ls_restr.type _refine_ls_restr.dev_ideal _refine_ls_restr.dev_ideal_target _refine_ls_restr.weight _refine_ls_restr.number _refine_ls_restr.pdbx_refine_id _refine_ls_restr.pdbx_restraint_function f_bond_d 0.011 ? ? 3425 'X-RAY DIFFRACTION' ? f_angle_d 1.268 ? ? 4681 'X-RAY DIFFRACTION' ? f_dihedral_angle_d 18.556 ? ? 1251 'X-RAY DIFFRACTION' ? f_chiral_restr 0.065 ? ? 564 'X-RAY DIFFRACTION' ? f_plane_restr 0.007 ? ? 584 'X-RAY DIFFRACTION' ? # loop_ _refine_ls_shell.pdbx_refine_id _refine_ls_shell.pdbx_total_number_of_bins_used _refine_ls_shell.d_res_high _refine_ls_shell.d_res_low _refine_ls_shell.number_reflns_R_work _refine_ls_shell.R_factor_R_work _refine_ls_shell.percent_reflns_obs _refine_ls_shell.R_factor_R_free _refine_ls_shell.R_factor_R_free_error _refine_ls_shell.percent_reflns_R_free _refine_ls_shell.number_reflns_R_free _refine_ls_shell.number_reflns_all _refine_ls_shell.R_factor_all _refine_ls_shell.R_factor_obs _refine_ls_shell.number_reflns_obs 'X-RAY DIFFRACTION' . 2.5801 2.6834 2643 0.2729 100.00 0.3343 . . 148 . . . . 'X-RAY DIFFRACTION' . 2.6834 2.8054 2656 0.2590 99.00 0.3058 . . 132 . . . . 'X-RAY DIFFRACTION' . 2.8054 2.9532 2620 0.2610 99.00 0.3102 . . 149 . . . . 'X-RAY DIFFRACTION' . 2.9532 3.1380 2679 0.2584 100.00 0.3254 . . 140 . . . . 'X-RAY DIFFRACTION' . 3.1380 3.3800 2655 0.2469 100.00 0.3071 . . 135 . . . . 'X-RAY DIFFRACTION' . 3.3800 3.7196 2654 0.2301 100.00 0.3048 . . 159 . . . . 'X-RAY DIFFRACTION' . 3.7196 4.2565 2656 0.2129 99.00 0.2792 . . 143 . . . . 'X-RAY DIFFRACTION' . 4.2565 5.3576 2695 0.1941 100.00 0.2400 . . 138 . . . . 'X-RAY DIFFRACTION' . 5.3576 29.7721 2754 0.2238 100.00 0.2750 . . 133 . . . . # _struct.entry_id 5B22 _struct.title 'Dimer structure of murine Nectin-3 D1D2' _struct.pdbx_descriptor Nectin-3 _struct.pdbx_model_details ? _struct.pdbx_formula_weight ? _struct.pdbx_formula_weight_method ? _struct.pdbx_model_type_details ? _struct.pdbx_CASP_flag ? # _struct_keywords.entry_id 5B22 _struct_keywords.text 'cell-adhesion, immuboglobulin-like domain, adherens janction, CELL ADHESION' _struct_keywords.pdbx_keywords 'CELL ADHESION' # loop_ _struct_asym.id _struct_asym.pdbx_blank_PDB_chainid_flag _struct_asym.pdbx_modified _struct_asym.entity_id _struct_asym.details A N N 1 ? B N N 1 ? C N N 2 ? D N N 2 ? E N N 3 ? F N N 2 ? G N N 2 ? H N N 3 ? I N N 4 ? J N N 4 ? # loop_ _struct_conf.conf_type_id _struct_conf.id _struct_conf.pdbx_PDB_helix_id _struct_conf.beg_label_comp_id _struct_conf.beg_label_asym_id _struct_conf.beg_label_seq_id _struct_conf.pdbx_beg_PDB_ins_code _struct_conf.end_label_comp_id _struct_conf.end_label_asym_id _struct_conf.end_label_seq_id _struct_conf.pdbx_end_PDB_ins_code _struct_conf.beg_auth_comp_id _struct_conf.beg_auth_asym_id _struct_conf.beg_auth_seq_id _struct_conf.end_auth_comp_id _struct_conf.end_auth_asym_id _struct_conf.end_auth_seq_id _struct_conf.pdbx_PDB_helix_class _struct_conf.details _struct_conf.pdbx_PDB_helix_length HELX_P HELX_P1 AA1 GLY A 58 ? GLN A 61 ? GLY A 57 GLN A 60 5 ? 4 HELX_P HELX_P2 AA2 GLY A 82 ? SER A 86 ? GLY A 81 SER A 85 5 ? 5 HELX_P HELX_P3 AA3 THR A 179 ? ARG A 183 ? THR A 178 ARG A 182 5 ? 5 HELX_P HELX_P4 AA4 GLY B 58 ? GLN B 61 ? GLY B 57 GLN B 60 5 ? 4 HELX_P HELX_P5 AA5 GLY B 82 ? SER B 86 ? GLY B 81 SER B 85 5 ? 5 # _struct_conf_type.id HELX_P _struct_conf_type.criteria ? _struct_conf_type.reference ? # loop_ _struct_conn.id _struct_conn.conn_type_id _struct_conn.pdbx_leaving_atom_flag _struct_conn.pdbx_PDB_id _struct_conn.ptnr1_label_asym_id _struct_conn.ptnr1_label_comp_id _struct_conn.ptnr1_label_seq_id _struct_conn.ptnr1_label_atom_id _struct_conn.pdbx_ptnr1_label_alt_id _struct_conn.pdbx_ptnr1_PDB_ins_code _struct_conn.pdbx_ptnr1_standard_comp_id _struct_conn.ptnr1_symmetry _struct_conn.ptnr2_label_asym_id _struct_conn.ptnr2_label_comp_id _struct_conn.ptnr2_label_seq_id _struct_conn.ptnr2_label_atom_id _struct_conn.pdbx_ptnr2_label_alt_id _struct_conn.pdbx_ptnr2_PDB_ins_code _struct_conn.ptnr1_auth_asym_id _struct_conn.ptnr1_auth_comp_id _struct_conn.ptnr1_auth_seq_id _struct_conn.ptnr2_auth_asym_id _struct_conn.ptnr2_auth_comp_id _struct_conn.ptnr2_auth_seq_id _struct_conn.ptnr2_symmetry _struct_conn.pdbx_ptnr3_label_atom_id _struct_conn.pdbx_ptnr3_label_seq_id _struct_conn.pdbx_ptnr3_label_comp_id _struct_conn.pdbx_ptnr3_label_asym_id _struct_conn.pdbx_ptnr3_label_alt_id _struct_conn.pdbx_ptnr3_PDB_ins_code _struct_conn.details _struct_conn.pdbx_dist_value _struct_conn.pdbx_value_order disulf1 disulf ? ? A CYS 21 SG ? ? ? 1_555 A CYS 91 SG ? ? A CYS 20 A CYS 90 1_555 ? ? ? ? ? ? ? 2.027 ? disulf2 disulf ? ? A CYS 136 SG ? ? ? 1_555 A CYS 189 SG ? ? A CYS 135 A CYS 188 1_555 ? ? ? ? ? ? ? 2.036 ? disulf3 disulf ? ? B CYS 21 SG ? ? ? 1_555 B CYS 91 SG ? ? B CYS 20 B CYS 90 1_555 ? ? ? ? ? ? ? 2.048 ? disulf4 disulf ? ? B CYS 136 SG ? ? ? 1_555 B CYS 189 SG ? ? B CYS 135 B CYS 188 1_555 ? ? ? ? ? ? ? 2.036 ? covale1 covale one ? A ASN 165 ND2 ? ? ? 1_555 C NAG . C1 ? ? A ASN 164 A NAG 301 1_555 ? ? ? ? ? ? ? 1.459 ? covale2 covale one ? B ASN 165 ND2 ? ? ? 1_555 F NAG . C1 ? ? B ASN 164 B NAG 301 1_555 ? ? ? ? ? ? ? 1.445 ? covale3 covale both ? C NAG . O4 ? ? ? 1_555 D NAG . C1 ? ? A NAG 301 A NAG 302 1_555 ? ? ? ? ? ? ? 1.452 ? covale4 covale both ? D NAG . O4 ? ? ? 1_555 E BMA . C1 ? ? A NAG 302 A BMA 303 1_555 ? ? ? ? ? ? ? 1.444 ? covale5 covale both ? F NAG . O4 ? ? ? 1_555 G NAG . C1 ? ? B NAG 301 B NAG 302 1_555 ? ? ? ? ? ? ? 1.427 ? covale6 covale both ? G NAG . O4 ? ? ? 1_555 H BMA . C1 ? ? B NAG 302 B BMA 303 1_555 ? ? ? ? ? ? ? 1.456 ? # loop_ _struct_conn_type.id _struct_conn_type.criteria _struct_conn_type.reference disulf ? ? covale ? ? # loop_ _struct_mon_prot_cis.pdbx_id _struct_mon_prot_cis.label_comp_id _struct_mon_prot_cis.label_seq_id _struct_mon_prot_cis.label_asym_id _struct_mon_prot_cis.label_alt_id _struct_mon_prot_cis.pdbx_PDB_ins_code _struct_mon_prot_cis.auth_comp_id _struct_mon_prot_cis.auth_seq_id _struct_mon_prot_cis.auth_asym_id _struct_mon_prot_cis.pdbx_label_comp_id_2 _struct_mon_prot_cis.pdbx_label_seq_id_2 _struct_mon_prot_cis.pdbx_label_asym_id_2 _struct_mon_prot_cis.pdbx_PDB_ins_code_2 _struct_mon_prot_cis.pdbx_auth_comp_id_2 _struct_mon_prot_cis.pdbx_auth_seq_id_2 _struct_mon_prot_cis.pdbx_auth_asym_id_2 _struct_mon_prot_cis.pdbx_PDB_model_num _struct_mon_prot_cis.pdbx_omega_angle 1 PHE 96 A . ? PHE 95 A PRO 97 A ? PRO 96 A 1 8.17 2 LYS 142 A . ? LYS 141 A PRO 143 A ? PRO 142 A 1 -3.56 3 PHE 96 B . ? PHE 95 B PRO 97 B ? PRO 96 B 1 0.22 4 LYS 142 B . ? LYS 141 B PRO 143 B ? PRO 142 B 1 -11.10 # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details AA1 ? 2 ? AA2 ? 6 ? AA3 ? 3 ? AA4 ? 4 ? AA5 ? 3 ? AA6 ? 2 ? AA7 ? 6 ? AA8 ? 3 ? AA9 ? 4 ? AB1 ? 2 ? AB2 ? 3 ? # loop_ _struct_sheet_order.sheet_id _struct_sheet_order.range_id_1 _struct_sheet_order.range_id_2 _struct_sheet_order.offset _struct_sheet_order.sense AA1 1 2 ? anti-parallel AA2 1 2 ? parallel AA2 2 3 ? anti-parallel AA2 3 4 ? anti-parallel AA2 4 5 ? anti-parallel AA2 5 6 ? anti-parallel AA3 1 2 ? anti-parallel AA3 2 3 ? anti-parallel AA4 1 2 ? anti-parallel AA4 2 3 ? anti-parallel AA4 3 4 ? anti-parallel AA5 1 2 ? anti-parallel AA5 2 3 ? anti-parallel AA6 1 2 ? anti-parallel AA7 1 2 ? parallel AA7 2 3 ? anti-parallel AA7 3 4 ? anti-parallel AA7 4 5 ? anti-parallel AA7 5 6 ? anti-parallel AA8 1 2 ? anti-parallel AA8 2 3 ? anti-parallel AA9 1 2 ? anti-parallel AA9 2 3 ? anti-parallel AA9 3 4 ? anti-parallel AB1 1 2 ? parallel AB2 1 2 ? anti-parallel AB2 2 3 ? anti-parallel # loop_ _struct_sheet_range.sheet_id _struct_sheet_range.id _struct_sheet_range.beg_label_comp_id _struct_sheet_range.beg_label_asym_id _struct_sheet_range.beg_label_seq_id _struct_sheet_range.pdbx_beg_PDB_ins_code _struct_sheet_range.end_label_comp_id _struct_sheet_range.end_label_asym_id _struct_sheet_range.end_label_seq_id _struct_sheet_range.pdbx_end_PDB_ins_code _struct_sheet_range.beg_auth_comp_id _struct_sheet_range.beg_auth_asym_id _struct_sheet_range.beg_auth_seq_id _struct_sheet_range.end_auth_comp_id _struct_sheet_range.end_auth_asym_id _struct_sheet_range.end_auth_seq_id AA1 1 ILE A 3 ? ILE A 4 ? ILE A 2 ILE A 3 AA1 2 LEU A 22 ? ILE A 23 ? LEU A 21 ILE A 22 AA2 1 HIS A 8 ? VAL A 12 ? HIS A 7 VAL A 11 AA2 2 GLY A 99 ? LEU A 110 ? GLY A 98 LEU A 109 AA2 3 GLY A 87 ? PHE A 96 ? GLY A 86 PHE A 95 AA2 4 THR A 28 ? HIS A 38 ? THR A 27 HIS A 37 AA2 5 SER A 41 ? HIS A 49 ? SER A 40 HIS A 48 AA2 6 GLY A 53 ? VAL A 56 ? GLY A 52 VAL A 55 AA3 1 VAL A 17 ? LEU A 19 ? VAL A 16 LEU A 18 AA3 2 ILE A 76 ? LEU A 78 ? ILE A 75 LEU A 77 AA3 3 VAL A 64 ? PHE A 66 ? VAL A 63 PHE A 65 AA4 1 THR A 114 ? ILE A 118 ? THR A 113 ILE A 117 AA4 2 THR A 131 ? GLY A 141 ? THR A 130 GLY A 140 AA4 3 ALA A 168 ? LEU A 176 ? ALA A 167 LEU A 175 AA4 4 GLU A 155 ? SER A 162 ? GLU A 154 SER A 161 AA5 1 GLN A 146 ? GLU A 150 ? GLN A 145 GLU A 149 AA5 2 ARG A 186 ? LYS A 192 ? ARG A 185 LYS A 191 AA5 3 ILE A 200 ? ILE A 205 ? ILE A 199 ILE A 204 AA6 1 ILE B 3 ? ILE B 4 ? ILE B 2 ILE B 3 AA6 2 LEU B 22 ? ILE B 23 ? LEU B 21 ILE B 22 AA7 1 HIS B 8 ? VAL B 12 ? HIS B 7 VAL B 11 AA7 2 GLY B 99 ? LEU B 110 ? GLY B 98 LEU B 109 AA7 3 GLY B 87 ? PHE B 96 ? GLY B 86 PHE B 95 AA7 4 THR B 28 ? HIS B 38 ? THR B 27 HIS B 37 AA7 5 SER B 41 ? HIS B 49 ? SER B 40 HIS B 48 AA7 6 GLY B 53 ? VAL B 56 ? GLY B 52 VAL B 55 AA8 1 VAL B 17 ? LEU B 19 ? VAL B 16 LEU B 18 AA8 2 ILE B 76 ? LEU B 78 ? ILE B 75 LEU B 77 AA8 3 VAL B 64 ? PHE B 66 ? VAL B 63 PHE B 65 AA9 1 THR B 114 ? LYS B 119 ? THR B 113 LYS B 118 AA9 2 THR B 131 ? GLY B 141 ? THR B 130 GLY B 140 AA9 3 ALA B 168 ? LEU B 176 ? ALA B 167 LEU B 175 AA9 4 GLU B 155 ? SER B 162 ? GLU B 154 SER B 161 AB1 1 LEU B 124 ? ILE B 125 ? LEU B 123 ILE B 124 AB1 2 ILE B 208 ? GLN B 209 ? ILE B 207 GLN B 208 AB2 1 GLN B 146 ? GLU B 150 ? GLN B 145 GLU B 149 AB2 2 ARG B 186 ? LYS B 192 ? ARG B 185 LYS B 191 AB2 3 ILE B 200 ? ILE B 205 ? ILE B 199 ILE B 204 # loop_ _pdbx_struct_sheet_hbond.sheet_id _pdbx_struct_sheet_hbond.range_id_1 _pdbx_struct_sheet_hbond.range_id_2 _pdbx_struct_sheet_hbond.range_1_label_atom_id _pdbx_struct_sheet_hbond.range_1_label_comp_id _pdbx_struct_sheet_hbond.range_1_label_asym_id _pdbx_struct_sheet_hbond.range_1_label_seq_id _pdbx_struct_sheet_hbond.range_1_PDB_ins_code _pdbx_struct_sheet_hbond.range_1_auth_atom_id _pdbx_struct_sheet_hbond.range_1_auth_comp_id _pdbx_struct_sheet_hbond.range_1_auth_asym_id _pdbx_struct_sheet_hbond.range_1_auth_seq_id _pdbx_struct_sheet_hbond.range_2_label_atom_id _pdbx_struct_sheet_hbond.range_2_label_comp_id _pdbx_struct_sheet_hbond.range_2_label_asym_id _pdbx_struct_sheet_hbond.range_2_label_seq_id _pdbx_struct_sheet_hbond.range_2_PDB_ins_code _pdbx_struct_sheet_hbond.range_2_auth_atom_id _pdbx_struct_sheet_hbond.range_2_auth_comp_id _pdbx_struct_sheet_hbond.range_2_auth_asym_id _pdbx_struct_sheet_hbond.range_2_auth_seq_id AA1 1 2 N ILE A 4 ? N ILE A 3 O LEU A 22 ? O LEU A 21 AA2 1 2 N VAL A 9 ? N VAL A 8 O THR A 106 ? O THR A 105 AA2 2 3 O THR A 105 ? O THR A 104 N TYR A 89 ? N TYR A 88 AA2 3 4 O PHE A 96 ? O PHE A 95 N THR A 28 ? N THR A 27 AA2 4 5 N LYS A 36 ? N LYS A 35 O GLN A 43 ? O GLN A 42 AA2 5 6 N VAL A 47 ? N VAL A 46 O SER A 55 ? O SER A 54 AA3 1 2 N LEU A 19 ? N LEU A 18 O ILE A 76 ? O ILE A 75 AA3 2 3 O THR A 77 ? O THR A 76 N LEU A 65 ? N LEU A 64 AA4 1 2 N THR A 114 ? N THR A 113 O ALA A 139 ? O ALA A 138 AA4 2 3 N CYS A 136 ? N CYS A 135 O SER A 172 ? O SER A 171 AA4 3 4 O GLN A 173 ? O GLN A 172 N GLU A 157 ? N GLU A 156 AA5 1 2 N ASP A 148 ? N ASP A 147 O VAL A 190 ? O VAL A 189 AA5 2 3 N CYS A 189 ? N CYS A 188 O TYR A 202 ? O TYR A 201 AA6 1 2 N ILE B 4 ? N ILE B 3 O LEU B 22 ? O LEU B 21 AA7 1 2 N ALA B 11 ? N ALA B 10 O LEU B 110 ? O LEU B 109 AA7 2 3 O VAL B 107 ? O VAL B 106 N GLY B 87 ? N GLY B 86 AA7 3 4 O LYS B 92 ? O LYS B 91 N SER B 33 ? N SER B 32 AA7 4 5 N TRP B 34 ? N TRP B 33 O VAL B 45 ? O VAL B 44 AA7 5 6 N VAL B 47 ? N VAL B 46 O SER B 55 ? O SER B 54 AA8 1 2 N LEU B 19 ? N LEU B 18 O ILE B 76 ? O ILE B 75 AA8 2 3 O THR B 77 ? O THR B 76 N LEU B 65 ? N LEU B 64 AA9 1 2 N ILE B 118 ? N ILE B 117 O VAL B 135 ? O VAL B 134 AA9 2 3 N CYS B 136 ? N CYS B 135 O SER B 172 ? O SER B 171 AA9 3 4 O GLN B 173 ? O GLN B 172 N GLU B 157 ? N GLU B 156 AB1 1 2 N LEU B 124 ? N LEU B 123 O GLN B 209 ? O GLN B 208 AB2 1 2 N ASP B 148 ? N ASP B 147 O VAL B 190 ? O VAL B 189 AB2 2 3 N CYS B 189 ? N CYS B 188 O TYR B 202 ? O TYR B 201 # loop_ _struct_site.id _struct_site.pdbx_evidence_code _struct_site.pdbx_auth_asym_id _struct_site.pdbx_auth_comp_id _struct_site.pdbx_auth_seq_id _struct_site.pdbx_auth_ins_code _struct_site.pdbx_num_residues _struct_site.details AC1 Software A ASN 164 ? 7 'binding site for Poly-Saccharide residues NAG A 301 through BMA A 303 bound to ASN A 164' AC2 Software B ASN 164 ? 13 'binding site for Poly-Saccharide residues NAG B 301 through BMA B 303 bound to ASN B 164' # loop_ _struct_site_gen.id _struct_site_gen.site_id _struct_site_gen.pdbx_num_res _struct_site_gen.label_comp_id _struct_site_gen.label_asym_id _struct_site_gen.label_seq_id _struct_site_gen.pdbx_auth_ins_code _struct_site_gen.auth_comp_id _struct_site_gen.auth_asym_id _struct_site_gen.auth_seq_id _struct_site_gen.label_atom_id _struct_site_gen.label_alt_id _struct_site_gen.symmetry _struct_site_gen.details 1 AC1 7 TRP A 13 ? TRP A 12 . ? 1_555 ? 2 AC1 7 PHE A 83 ? PHE A 82 . ? 1_555 ? 3 AC1 7 PHE A 163 ? PHE A 162 . ? 1_555 ? 4 AC1 7 ASN A 165 ? ASN A 164 . ? 1_555 ? 5 AC1 7 THR A 167 ? THR A 166 . ? 1_555 ? 6 AC1 7 HOH I . ? HOH A 429 . ? 1_555 ? 7 AC1 7 HOH I . ? HOH A 433 . ? 1_555 ? 8 AC2 13 TRP B 13 ? TRP B 12 . ? 1_555 ? 9 AC2 13 PHE B 83 ? PHE B 82 . ? 1_555 ? 10 AC2 13 THR B 140 ? THR B 139 . ? 1_555 ? 11 AC2 13 PHE B 163 ? PHE B 162 . ? 1_555 ? 12 AC2 13 ASN B 165 ? ASN B 164 . ? 1_555 ? 13 AC2 13 THR B 167 ? THR B 166 . ? 1_555 ? 14 AC2 13 HOH J . ? HOH B 411 . ? 1_555 ? 15 AC2 13 HOH J . ? HOH B 414 . ? 1_555 ? 16 AC2 13 HOH J . ? HOH B 433 . ? 1_555 ? 17 AC2 13 HOH J . ? HOH B 447 . ? 1_555 ? 18 AC2 13 HOH J . ? HOH B 455 . ? 1_555 ? 19 AC2 13 HOH J . ? HOH B 456 . ? 1_555 ? 20 AC2 13 HOH J . ? HOH B 471 . ? 1_555 ? # _atom_sites.entry_id 5B22 _atom_sites.fract_transf_matrix[1][1] 0.006594 _atom_sites.fract_transf_matrix[1][2] 0.000000 _atom_sites.fract_transf_matrix[1][3] 0.003268 _atom_sites.fract_transf_matrix[2][1] 0.000000 _atom_sites.fract_transf_matrix[2][2] 0.013721 _atom_sites.fract_transf_matrix[2][3] 0.000000 _atom_sites.fract_transf_matrix[3][1] 0.000000 _atom_sites.fract_transf_matrix[3][2] 0.000000 _atom_sites.fract_transf_matrix[3][3] 0.013622 _atom_sites.fract_transf_vector[1] 0.00000 _atom_sites.fract_transf_vector[2] 0.00000 _atom_sites.fract_transf_vector[3] 0.00000 # loop_ _atom_type.symbol C N O S # loop_ _atom_site.group_PDB _atom_site.id _atom_site.type_symbol _atom_site.label_atom_id _atom_site.label_alt_id _atom_site.label_comp_id _atom_site.label_asym_id _atom_site.label_entity_id _atom_site.label_seq_id _atom_site.pdbx_PDB_ins_code _atom_site.Cartn_x _atom_site.Cartn_y _atom_site.Cartn_z _atom_site.occupancy _atom_site.B_iso_or_equiv _atom_site.pdbx_formal_charge _atom_site.auth_seq_id _atom_site.auth_comp_id _atom_site.auth_asym_id _atom_site.auth_atom_id _atom_site.pdbx_PDB_model_num ATOM 1 N N . PRO A 1 1 ? 32.908 5.740 23.771 1.00 58.26 ? 0 PRO A N 1 ATOM 2 C CA . PRO A 1 1 ? 32.588 6.952 24.533 1.00 73.15 ? 0 PRO A CA 1 ATOM 3 C C . PRO A 1 1 ? 33.473 7.141 25.759 1.00 74.08 ? 0 PRO A C 1 ATOM 4 O O . PRO A 1 1 ? 34.687 7.305 25.635 1.00 73.31 ? 0 PRO A O 1 ATOM 5 C CB . PRO A 1 1 ? 31.123 6.727 24.932 1.00 58.00 ? 0 PRO A CB 1 ATOM 6 C CG . PRO A 1 1 ? 30.560 5.884 23.776 1.00 67.39 ? 0 PRO A CG 1 ATOM 7 C CD . PRO A 1 1 ? 31.743 5.284 22.996 1.00 59.82 ? 0 PRO A CD 1 ATOM 8 N N . SER A 1 2 ? 32.862 7.132 26.937 1.00 69.62 ? 1 SER A N 1 ATOM 9 C CA . SER A 1 2 ? 33.605 7.134 28.191 1.00 73.73 ? 1 SER A CA 1 ATOM 10 C C . SER A 1 2 ? 33.900 5.722 28.701 1.00 73.14 ? 1 SER A C 1 ATOM 11 O O . SER A 1 2 ? 34.249 5.555 29.876 1.00 59.50 ? 1 SER A O 1 ATOM 12 C CB . SER A 1 2 ? 32.831 7.925 29.241 1.00 73.77 ? 1 SER A CB 1 ATOM 13 O OG . SER A 1 2 ? 31.435 7.732 29.065 1.00 86.28 ? 1 SER A OG 1 ATOM 14 N N . ILE A 1 3 ? 33.768 4.713 27.845 1.00 72.52 ? 2 ILE A N 1 ATOM 15 C CA . ILE A 1 3 ? 33.945 3.315 28.219 1.00 68.14 ? 2 ILE A CA 1 ATOM 16 C C . ILE A 1 3 ? 35.309 2.873 27.697 1.00 54.79 ? 2 ILE A C 1 ATOM 17 O O . ILE A 1 3 ? 35.529 2.810 26.483 1.00 62.19 ? 2 ILE A O 1 ATOM 18 C CB . ILE A 1 3 ? 32.815 2.436 27.658 1.00 65.22 ? 2 ILE A CB 1 ATOM 19 C CG1 . ILE A 1 3 ? 31.450 3.148 27.738 1.00 56.89 ? 2 ILE A CG1 1 ATOM 20 C CG2 . ILE A 1 3 ? 32.771 1.103 28.390 1.00 60.76 ? 2 ILE A CG2 1 ATOM 21 C CD1 . ILE A 1 3 ? 30.927 3.388 29.138 1.00 48.84 ? 2 ILE A CD1 1 ATOM 22 N N . ILE A 1 4 ? 36.227 2.547 28.599 1.00 48.34 ? 3 ILE A N 1 ATOM 23 C CA . ILE A 1 4 ? 37.596 2.203 28.220 1.00 56.88 ? 3 ILE A CA 1 ATOM 24 C C . ILE A 1 4 ? 37.731 0.687 28.084 1.00 52.16 ? 3 ILE A C 1 ATOM 25 O O . ILE A 1 4 ? 37.651 -0.044 29.072 1.00 46.68 ? 3 ILE A O 1 ATOM 26 C CB . ILE A 1 4 ? 38.604 2.741 29.240 1.00 60.08 ? 3 ILE A CB 1 ATOM 27 C CG1 . ILE A 1 4 ? 38.406 4.250 29.452 1.00 66.92 ? 3 ILE A CG1 1 ATOM 28 C CG2 . ILE A 1 4 ? 40.011 2.384 28.806 1.00 53.14 ? 3 ILE A CG2 1 ATOM 29 C CD1 . ILE A 1 4 ? 38.531 5.083 28.193 1.00 70.92 ? 3 ILE A CD1 1 ATOM 30 N N . VAL A 1 5 ? 37.974 0.211 26.862 1.00 47.54 ? 4 VAL A N 1 ATOM 31 C CA . VAL A 1 5 ? 38.143 -1.207 26.592 1.00 45.65 ? 4 VAL A CA 1 ATOM 32 C C . VAL A 1 5 ? 39.251 -1.400 25.563 1.00 53.02 ? 4 VAL A C 1 ATOM 33 O O . VAL A 1 5 ? 39.853 -0.448 25.056 1.00 57.18 ? 4 VAL A O 1 ATOM 34 C CB . VAL A 1 5 ? 36.845 -1.874 26.083 1.00 45.21 ? 4 VAL A CB 1 ATOM 35 C CG1 . VAL A 1 5 ? 35.739 -1.803 27.128 1.00 43.45 ? 4 VAL A CG1 1 ATOM 36 C CG2 . VAL A 1 5 ? 36.406 -1.234 24.782 1.00 47.16 ? 4 VAL A CG2 1 ATOM 37 N N . GLU A 1 6 ? 39.510 -2.665 25.254 1.00 54.03 ? 5 GLU A N 1 ATOM 38 C CA . GLU A 1 6 ? 40.500 -2.983 24.203 1.00 51.51 ? 5 GLU A CA 1 ATOM 39 C C . GLU A 1 6 ? 39.755 -3.297 22.923 1.00 49.56 ? 5 GLU A C 1 ATOM 40 O O . GLU A 1 6 ? 38.701 -3.913 22.992 1.00 47.24 ? 5 GLU A O 1 ATOM 41 C CB . GLU A 1 6 ? 41.359 -4.179 24.656 1.00 43.41 ? 5 GLU A CB 1 ATOM 42 C CG . GLU A 1 6 ? 42.859 -4.173 24.286 1.00 58.87 ? 5 GLU A CG 1 ATOM 43 C CD . GLU A 1 6 ? 43.214 -4.159 22.812 1.00 69.86 ? 5 GLU A CD 1 ATOM 44 O OE1 . GLU A 1 6 ? 42.583 -4.829 22.013 1.00 75.72 ? 5 GLU A OE1 1 ATOM 45 O OE2 . GLU A 1 6 ? 44.160 -3.486 22.394 1.00 75.12 ? 5 GLU A OE2 1 ATOM 46 N N . PRO A 1 7 ? 40.139 -2.783 21.740 1.00 60.30 ? 6 PRO A N 1 ATOM 47 C CA . PRO A 1 7 ? 39.349 -3.049 20.568 1.00 56.64 ? 6 PRO A CA 1 ATOM 48 C C . PRO A 1 7 ? 39.254 -4.507 20.188 1.00 49.05 ? 6 PRO A C 1 ATOM 49 O O . PRO A 1 7 ? 38.167 -4.944 19.745 1.00 53.12 ? 6 PRO A O 1 ATOM 50 C CB . PRO A 1 7 ? 40.091 -2.273 19.491 1.00 63.52 ? 6 PRO A CB 1 ATOM 51 C CG . PRO A 1 7 ? 41.593 -2.140 20.088 1.00 61.93 ? 6 PRO A CG 1 ATOM 52 C CD . PRO A 1 7 ? 41.064 -1.737 21.417 1.00 65.37 ? 6 PRO A CD 1 ATOM 53 N N . HIS A 1 8 ? 40.300 -5.285 20.389 1.00 50.49 ? 7 HIS A N 1 ATOM 54 C CA . HIS A 1 8 ? 40.372 -6.645 19.880 1.00 53.21 ? 7 HIS A CA 1 ATOM 55 C C . HIS A 1 8 ? 41.156 -7.525 20.836 1.00 41.48 ? 7 HIS A C 1 ATOM 56 O O . HIS A 1 8 ? 42.246 -7.166 21.265 1.00 47.56 ? 7 HIS A O 1 ATOM 57 C CB . HIS A 1 8 ? 41.026 -6.678 18.486 1.00 55.84 ? 7 HIS A CB 1 ATOM 58 C CG . HIS A 1 8 ? 40.181 -6.075 17.407 1.00 59.73 ? 7 HIS A CG 1 ATOM 59 N ND1 . HIS A 1 8 ? 40.013 -4.713 17.264 1.00 66.63 ? 7 HIS A ND1 1 ATOM 60 C CD2 . HIS A 1 8 ? 39.427 -6.650 16.440 1.00 60.69 ? 7 HIS A CD2 1 ATOM 61 C CE1 . HIS A 1 8 ? 39.195 -4.475 16.254 1.00 67.55 ? 7 HIS A CE1 1 ATOM 62 N NE2 . HIS A 1 8 ? 38.825 -5.634 15.736 1.00 69.16 ? 7 HIS A NE2 1 ATOM 63 N N . VAL A 1 9 ? 40.644 -8.698 21.144 1.00 42.11 ? 8 VAL A N 1 ATOM 64 C CA . VAL A 1 9 ? 41.346 -9.563 22.084 1.00 36.16 ? 8 VAL A CA 1 ATOM 65 C C . VAL A 1 9 ? 41.501 -10.944 21.464 1.00 38.53 ? 8 VAL A C 1 ATOM 66 O O . VAL A 1 9 ? 40.594 -11.434 20.777 1.00 40.31 ? 8 VAL A O 1 ATOM 67 C CB . VAL A 1 9 ? 40.610 -9.605 23.437 1.00 40.22 ? 8 VAL A CB 1 ATOM 68 C CG1 . VAL A 1 9 ? 41.000 -10.815 24.232 1.00 37.39 ? 8 VAL A CG1 1 ATOM 69 C CG2 . VAL A 1 9 ? 40.877 -8.317 24.217 1.00 47.17 ? 8 VAL A CG2 1 ATOM 70 N N . THR A 1 10 ? 42.673 -11.538 21.645 1.00 39.32 ? 9 THR A N 1 ATOM 71 C CA . THR A 1 10 ? 42.915 -12.908 21.225 1.00 32.92 ? 9 THR A CA 1 ATOM 72 C C . THR A 1 10 ? 42.818 -13.831 22.425 1.00 32.74 ? 9 THR A C 1 ATOM 73 O O . THR A 1 10 ? 43.342 -13.535 23.495 1.00 33.06 ? 9 THR A O 1 ATOM 74 C CB . THR A 1 10 ? 44.273 -13.056 20.568 1.00 25.87 ? 9 THR A CB 1 ATOM 75 O OG1 . THR A 1 10 ? 44.305 -12.209 19.424 1.00 39.75 ? 9 THR A OG1 1 ATOM 76 C CG2 . THR A 1 10 ? 44.456 -14.448 20.119 1.00 33.03 ? 9 THR A CG2 1 ATOM 77 N N . ALA A 1 11 ? 42.126 -14.939 22.237 1.00 32.63 ? 10 ALA A N 1 ATOM 78 C CA . ALA A 1 11 ? 41.761 -15.850 23.302 1.00 22.69 ? 10 ALA A CA 1 ATOM 79 C C . ALA A 1 11 ? 42.082 -17.244 22.821 1.00 29.20 ? 10 ALA A C 1 ATOM 80 O O . ALA A 1 11 ? 41.812 -17.577 21.663 1.00 32.14 ? 10 ALA A O 1 ATOM 81 C CB . ALA A 1 11 ? 40.274 -15.754 23.617 1.00 28.06 ? 10 ALA A CB 1 ATOM 82 N N . VAL A 1 12 ? 42.645 -18.056 23.692 1.00 26.84 ? 11 VAL A N 1 ATOM 83 C CA . VAL A 1 12 ? 43.104 -19.371 23.289 1.00 24.67 ? 11 VAL A CA 1 ATOM 84 C C . VAL A 1 12 ? 42.155 -20.398 23.861 1.00 28.46 ? 11 VAL A C 1 ATOM 85 O O . VAL A 1 12 ? 41.765 -20.321 25.033 1.00 26.30 ? 11 VAL A O 1 ATOM 86 C CB . VAL A 1 12 ? 44.559 -19.616 23.725 1.00 31.98 ? 11 VAL A CB 1 ATOM 87 C CG1 . VAL A 1 12 ? 45.010 -21.026 23.326 1.00 27.03 ? 11 VAL A CG1 1 ATOM 88 C CG2 . VAL A 1 12 ? 45.461 -18.574 23.072 1.00 19.21 ? 11 VAL A CG2 1 ATOM 89 N N . TRP A 1 13 ? 41.759 -21.343 23.013 1.00 25.88 ? 12 TRP A N 1 ATOM 90 C CA . TRP A 1 13 ? 40.771 -22.339 23.391 1.00 26.43 ? 12 TRP A CA 1 ATOM 91 C C . TRP A 1 13 ? 41.250 -23.111 24.613 1.00 28.11 ? 12 TRP A C 1 ATOM 92 O O . TRP A 1 13 ? 42.404 -23.539 24.677 1.00 29.02 ? 12 TRP A O 1 ATOM 93 C CB . TRP A 1 13 ? 40.518 -23.274 22.212 1.00 21.27 ? 12 TRP A CB 1 ATOM 94 C CG . TRP A 1 13 ? 39.362 -24.216 22.379 1.00 31.50 ? 12 TRP A CG 1 ATOM 95 C CD1 . TRP A 1 13 ? 38.133 -24.093 21.812 1.00 28.93 ? 12 TRP A CD1 1 ATOM 96 C CD2 . TRP A 1 13 ? 39.329 -25.448 23.140 1.00 22.92 ? 12 TRP A CD2 1 ATOM 97 N NE1 . TRP A 1 13 ? 37.341 -25.165 22.160 1.00 24.83 ? 12 TRP A NE1 1 ATOM 98 C CE2 . TRP A 1 13 ? 38.045 -25.999 22.985 1.00 22.29 ? 12 TRP A CE2 1 ATOM 99 C CE3 . TRP A 1 13 ? 40.253 -26.121 23.936 1.00 24.20 ? 12 TRP A CE3 1 ATOM 100 C CZ2 . TRP A 1 13 ? 37.660 -27.192 23.596 1.00 27.98 ? 12 TRP A CZ2 1 ATOM 101 C CZ3 . TRP A 1 13 ? 39.864 -27.319 24.547 1.00 29.90 ? 12 TRP A CZ3 1 ATOM 102 C CH2 . TRP A 1 13 ? 38.585 -27.838 24.370 1.00 23.88 ? 12 TRP A CH2 1 ATOM 103 N N . GLY A 1 14 ? 40.341 -23.228 25.629 1.00 33.52 ? 13 GLY A N 1 ATOM 104 C CA . GLY A 1 14 ? 40.673 -23.975 26.824 1.00 28.30 ? 13 GLY A CA 1 ATOM 105 C C . GLY A 1 14 ? 41.362 -23.186 27.920 1.00 33.78 ? 13 GLY A C 1 ATOM 106 O O . GLY A 1 14 ? 41.484 -23.705 29.041 1.00 29.41 ? 13 GLY A O 1 ATOM 107 N N . LYS A 1 15 ? 41.712 -21.946 27.624 1.00 32.27 ? 14 LYS A N 1 ATOM 108 C CA . LYS A 1 15 ? 42.395 -21.054 28.526 1.00 30.72 ? 14 LYS A CA 1 ATOM 109 C C . LYS A 1 15 ? 41.583 -19.884 29.027 1.00 30.23 ? 14 LYS A C 1 ATOM 110 O O . LYS A 1 15 ? 40.407 -19.952 29.096 1.00 27.45 ? 14 LYS A O 1 ATOM 111 C CB . LYS A 1 15 ? 43.653 -20.565 27.864 1.00 29.75 ? 14 LYS A CB 1 ATOM 112 C CG . LYS A 1 15 ? 44.531 -21.692 27.429 1.00 28.29 ? 14 LYS A CG 1 ATOM 113 C CD . LYS A 1 15 ? 45.972 -21.291 27.453 1.00 28.06 ? 14 LYS A CD 1 ATOM 114 C CE . LYS A 1 15 ? 46.855 -22.362 26.878 1.00 41.35 ? 14 LYS A CE 1 ATOM 115 N NZ . LYS A 1 15 ? 47.028 -23.502 27.792 1.00 38.14 ? 14 LYS A NZ 1 ATOM 116 N N . ASN A 1 16 ? 42.267 -18.813 29.393 1.00 35.75 ? 15 ASN A N 1 ATOM 117 C CA . ASN A 1 16 ? 41.677 -17.661 30.066 1.00 29.12 ? 15 ASN A CA 1 ATOM 118 C C . ASN A 1 16 ? 41.912 -16.401 29.237 1.00 34.15 ? 15 ASN A C 1 ATOM 119 O O . ASN A 1 16 ? 42.846 -16.332 28.433 1.00 25.45 ? 15 ASN A O 1 ATOM 120 C CB . ASN A 1 16 ? 42.289 -17.440 31.461 1.00 22.57 ? 15 ASN A CB 1 ATOM 121 C CG . ASN A 1 16 ? 42.190 -18.640 32.339 1.00 37.10 ? 15 ASN A CG 1 ATOM 122 O OD1 . ASN A 1 16 ? 41.299 -19.477 32.171 1.00 44.03 ? 15 ASN A OD1 1 ATOM 123 N ND2 . ASN A 1 16 ? 43.091 -18.733 33.315 1.00 44.09 ? 15 ASN A ND2 1 ATOM 124 N N . VAL A 1 17 ? 41.039 -15.405 29.436 1.00 28.71 ? 16 VAL A N 1 ATOM 125 C CA . VAL A 1 17 ? 41.256 -14.044 28.958 1.00 32.60 ? 16 VAL A CA 1 ATOM 126 C C . VAL A 1 17 ? 40.622 -13.079 29.944 1.00 35.29 ? 16 VAL A C 1 ATOM 127 O O . VAL A 1 17 ? 39.749 -13.442 30.732 1.00 33.11 ? 16 VAL A O 1 ATOM 128 C CB . VAL A 1 17 ? 40.662 -13.717 27.568 1.00 39.23 ? 16 VAL A CB 1 ATOM 129 C CG1 . VAL A 1 17 ? 41.373 -14.465 26.512 1.00 35.66 ? 16 VAL A CG1 1 ATOM 130 C CG2 . VAL A 1 17 ? 39.136 -13.908 27.557 1.00 22.15 ? 16 VAL A CG2 1 ATOM 131 N N . SER A 1 18 ? 41.064 -11.832 29.873 1.00 36.89 ? 17 SER A N 1 ATOM 132 C CA . SER A 1 18 ? 40.455 -10.718 30.573 1.00 35.71 ? 17 SER A CA 1 ATOM 133 C C . SER A 1 18 ? 39.743 -9.845 29.561 1.00 34.20 ? 17 SER A C 1 ATOM 134 O O . SER A 1 18 ? 40.303 -9.518 28.514 1.00 33.38 ? 17 SER A O 1 ATOM 135 C CB . SER A 1 18 ? 41.501 -9.898 31.322 1.00 37.23 ? 17 SER A CB 1 ATOM 136 O OG . SER A 1 18 ? 41.851 -10.553 32.520 1.00 47.09 ? 17 SER A OG 1 ATOM 137 N N . LEU A 1 19 ? 38.513 -9.495 29.856 1.00 31.77 ? 18 LEU A N 1 ATOM 138 C CA . LEU A 1 19 ? 37.809 -8.485 29.087 1.00 33.62 ? 18 LEU A CA 1 ATOM 139 C C . LEU A 1 19 ? 37.811 -7.254 29.971 1.00 36.56 ? 18 LEU A C 1 ATOM 140 O O . LEU A 1 19 ? 37.161 -7.235 31.020 1.00 33.17 ? 18 LEU A O 1 ATOM 141 C CB . LEU A 1 19 ? 36.402 -8.933 28.706 1.00 31.85 ? 18 LEU A CB 1 ATOM 142 C CG . LEU A 1 19 ? 36.360 -10.074 27.694 1.00 33.83 ? 18 LEU A CG 1 ATOM 143 C CD1 . LEU A 1 19 ? 34.999 -10.159 27.050 1.00 32.25 ? 18 LEU A CD1 1 ATOM 144 C CD2 . LEU A 1 19 ? 37.436 -9.859 26.645 1.00 38.94 ? 18 LEU A CD2 1 ATOM 145 N N . LYS A 1 20 ? 38.610 -6.265 29.584 1.00 41.26 ? 19 LYS A N 1 ATOM 146 C CA . LYS A 1 20 ? 38.858 -5.091 30.402 1.00 44.04 ? 19 LYS A CA 1 ATOM 147 C C . LYS A 1 20 ? 37.804 -4.023 30.137 1.00 40.78 ? 19 LYS A C 1 ATOM 148 O O . LYS A 1 20 ? 37.384 -3.808 28.994 1.00 38.22 ? 19 LYS A O 1 ATOM 149 C CB . LYS A 1 20 ? 40.256 -4.544 30.115 1.00 45.48 ? 19 LYS A CB 1 ATOM 150 C CG . LYS A 1 20 ? 40.428 -3.044 30.349 1.00 52.12 ? 19 LYS A CG 1 ATOM 151 C CD . LYS A 1 20 ? 41.363 -2.465 29.302 1.00 60.26 ? 19 LYS A CD 1 ATOM 152 C CE . LYS A 1 20 ? 41.949 -1.136 29.734 1.00 62.14 ? 19 LYS A CE 1 ATOM 153 N NZ . LYS A 1 20 ? 42.937 -0.637 28.725 1.00 50.42 ? 19 LYS A NZ 1 ATOM 154 N N . CYS A 1 21 ? 37.363 -3.366 31.203 1.00 36.86 ? 20 CYS A N 1 ATOM 155 C CA . CYS A 1 21 ? 36.411 -2.277 31.032 1.00 39.26 ? 20 CYS A CA 1 ATOM 156 C C . CYS A 1 21 ? 36.470 -1.384 32.262 1.00 41.41 ? 20 CYS A C 1 ATOM 157 O O . CYS A 1 21 ? 36.138 -1.827 33.364 1.00 46.45 ? 20 CYS A O 1 ATOM 158 C CB . CYS A 1 21 ? 35.021 -2.821 30.814 1.00 39.26 ? 20 CYS A CB 1 ATOM 159 S SG . CYS A 1 21 ? 33.887 -1.530 30.531 1.00 49.49 ? 20 CYS A SG 1 ATOM 160 N N . LEU A 1 22 ? 36.912 -0.148 32.075 1.00 42.87 ? 21 LEU A N 1 ATOM 161 C CA . LEU A 1 22 ? 36.961 0.854 33.134 1.00 51.11 ? 21 LEU A CA 1 ATOM 162 C C . LEU A 1 22 ? 35.948 1.943 32.825 1.00 51.87 ? 21 LEU A C 1 ATOM 163 O O . LEU A 1 22 ? 35.880 2.426 31.686 1.00 49.83 ? 21 LEU A O 1 ATOM 164 C CB . LEU A 1 22 ? 38.360 1.459 33.253 1.00 52.00 ? 21 LEU A CB 1 ATOM 165 C CG . LEU A 1 22 ? 39.420 0.481 33.759 1.00 43.03 ? 21 LEU A CG 1 ATOM 166 C CD1 . LEU A 1 22 ? 40.764 1.166 33.817 1.00 55.81 ? 21 LEU A CD1 1 ATOM 167 C CD2 . LEU A 1 22 ? 38.991 -0.155 35.095 1.00 47.32 ? 21 LEU A CD2 1 ATOM 168 N N . ILE A 1 23 ? 35.156 2.314 33.826 1.00 47.72 ? 22 ILE A N 1 ATOM 169 C CA . ILE A 1 23 ? 34.030 3.222 33.630 1.00 63.18 ? 22 ILE A CA 1 ATOM 170 C C . ILE A 1 23 ? 34.174 4.384 34.601 1.00 71.60 ? 22 ILE A C 1 ATOM 171 O O . ILE A 1 23 ? 34.093 4.187 35.814 1.00 69.18 ? 22 ILE A O 1 ATOM 172 C CB . ILE A 1 23 ? 32.680 2.530 33.854 1.00 60.05 ? 22 ILE A CB 1 ATOM 173 C CG1 . ILE A 1 23 ? 32.582 1.226 33.087 1.00 43.82 ? 22 ILE A CG1 1 ATOM 174 C CG2 . ILE A 1 23 ? 31.549 3.473 33.478 1.00 55.99 ? 22 ILE A CG2 1 ATOM 175 C CD1 . ILE A 1 23 ? 31.436 0.413 33.575 1.00 40.88 ? 22 ILE A CD1 1 ATOM 176 N N . GLU A 1 24 ? 34.363 5.584 34.090 1.00 68.37 ? 23 GLU A N 1 ATOM 177 C CA . GLU A 1 24 ? 34.214 6.761 34.946 1.00 78.70 ? 23 GLU A CA 1 ATOM 178 C C . GLU A 1 24 ? 33.467 7.775 34.069 1.00 81.69 ? 23 GLU A C 1 ATOM 179 O O . GLU A 1 24 ? 34.079 8.657 33.483 1.00 80.37 ? 23 GLU A O 1 ATOM 180 C CB . GLU A 1 24 ? 35.553 7.308 35.490 1.00 83.77 ? 23 GLU A CB 1 ATOM 181 C CG . GLU A 1 24 ? 35.364 8.640 36.254 1.00 94.09 ? 23 GLU A CG 1 ATOM 182 C CD . GLU A 1 24 ? 35.238 8.475 37.740 1.00 92.62 ? 23 GLU A CD 1 ATOM 183 O OE1 . GLU A 1 24 ? 35.429 7.376 38.263 1.00 110.75 ? 23 GLU A OE1 1 ATOM 184 O OE2 . GLU A 1 24 ? 34.978 9.471 38.416 1.00 90.87 ? 23 GLU A OE2 1 ATOM 185 N N . VAL A 1 25 ? 32.138 7.619 33.981 1.00 81.62 ? 24 VAL A N 1 ATOM 186 C CA . VAL A 1 25 ? 31.353 8.449 33.048 1.00 87.63 ? 24 VAL A CA 1 ATOM 187 C C . VAL A 1 25 ? 31.043 9.841 33.578 1.00 89.82 ? 24 VAL A C 1 ATOM 188 O O . VAL A 1 25 ? 30.617 10.677 32.787 1.00 89.25 ? 24 VAL A O 1 ATOM 189 C CB . VAL A 1 25 ? 30.036 7.758 32.618 1.00 79.54 ? 24 VAL A CB 1 ATOM 190 C CG1 . VAL A 1 25 ? 29.299 8.552 31.518 1.00 75.68 ? 24 VAL A CG1 1 ATOM 191 C CG2 . VAL A 1 25 ? 30.311 6.398 32.031 1.00 72.59 ? 24 VAL A CG2 1 ATOM 192 N N . ASN A 1 26 ? 31.455 10.198 34.881 1.00 76.95 ? 25 ASN A N 1 ATOM 193 C CA . ASN A 1 26 ? 31.060 11.388 35.676 1.00 73.00 ? 25 ASN A CA 1 ATOM 194 C C . ASN A 1 26 ? 29.755 11.256 36.450 1.00 76.95 ? 25 ASN A C 1 ATOM 195 O O . ASN A 1 26 ? 29.460 12.171 37.260 1.00 73.01 ? 25 ASN A O 1 ATOM 196 C CB . ASN A 1 26 ? 30.966 12.675 34.848 1.00 83.08 ? 25 ASN A CB 1 ATOM 197 C CG . ASN A 1 26 ? 29.712 12.752 34.004 1.00 96.82 ? 25 ASN A CG 1 ATOM 198 O OD1 . ASN A 1 26 ? 28.580 12.700 34.469 1.00 90.16 ? 25 ASN A OD1 1 ATOM 199 N ND2 . ASN A 1 26 ? 29.935 12.827 32.721 1.00 96.75 ? 25 ASN A ND2 1 ATOM 200 N N . GLU A 1 27 ? 28.857 10.385 36.373 1.00 76.37 ? 26 GLU A N 1 ATOM 201 C CA . GLU A 1 27 ? 27.548 10.491 37.005 1.00 60.48 ? 26 GLU A CA 1 ATOM 202 C C . GLU A 1 27 ? 27.149 9.158 37.603 1.00 47.84 ? 26 GLU A C 1 ATOM 203 O O . GLU A 1 27 ? 27.806 8.148 37.412 1.00 51.56 ? 26 GLU A O 1 ATOM 204 C CB . GLU A 1 27 ? 26.482 10.979 36.026 1.00 56.31 ? 26 GLU A CB 1 ATOM 205 C CG . GLU A 1 27 ? 26.177 10.031 34.916 1.00 58.29 ? 26 GLU A CG 1 ATOM 206 C CD . GLU A 1 27 ? 25.187 10.653 33.969 1.00 64.22 ? 26 GLU A CD 1 ATOM 207 O OE1 . GLU A 1 27 ? 24.061 10.108 33.804 1.00 51.41 ? 26 GLU A OE1 1 ATOM 208 O OE2 . GLU A 1 27 ? 25.543 11.724 33.419 1.00 66.90 ? 26 GLU A OE2 1 ATOM 209 N N . THR A 1 28 ? 26.041 9.166 38.337 1.00 46.24 ? 27 THR A N 1 ATOM 210 C CA . THR A 1 28 ? 25.662 7.995 39.109 1.00 43.47 ? 27 THR A CA 1 ATOM 211 C C . THR A 1 28 ? 25.389 6.788 38.208 1.00 47.68 ? 27 THR A C 1 ATOM 212 O O . THR A 1 28 ? 24.639 6.867 37.226 1.00 34.88 ? 27 THR A O 1 ATOM 213 C CB . THR A 1 28 ? 24.453 8.333 39.960 1.00 43.19 ? 27 THR A CB 1 ATOM 214 O OG1 . THR A 1 28 ? 24.643 9.634 40.514 1.00 60.90 ? 27 THR A OG1 1 ATOM 215 C CG2 . THR A 1 28 ? 24.330 7.355 41.100 1.00 49.77 ? 27 THR A CG2 1 ATOM 216 N N . ILE A 1 29 ? 26.030 5.669 38.539 1.00 49.54 ? 28 ILE A N 1 ATOM 217 C CA . ILE A 1 29 ? 25.983 4.451 37.736 1.00 39.27 ? 28 ILE A CA 1 ATOM 218 C C . ILE A 1 29 ? 24.935 3.544 38.332 1.00 33.02 ? 28 ILE A C 1 ATOM 219 O O . ILE A 1 29 ? 25.024 3.190 39.510 1.00 34.87 ? 28 ILE A O 1 ATOM 220 C CB . ILE A 1 29 ? 27.348 3.753 37.692 1.00 41.29 ? 28 ILE A CB 1 ATOM 221 C CG1 . ILE A 1 29 ? 28.324 4.579 36.849 1.00 45.28 ? 28 ILE A CG1 1 ATOM 222 C CG2 . ILE A 1 29 ? 27.201 2.354 37.148 1.00 40.61 ? 28 ILE A CG2 1 ATOM 223 C CD1 . ILE A 1 29 ? 29.656 3.921 36.639 1.00 46.09 ? 28 ILE A CD1 1 ATOM 224 N N . THR A 1 30 ? 23.930 3.189 37.531 1.00 33.07 ? 29 THR A N 1 ATOM 225 C CA . THR A 1 30 ? 22.854 2.346 38.024 1.00 30.28 ? 29 THR A CA 1 ATOM 226 C C . THR A 1 30 ? 23.141 0.857 37.832 1.00 37.28 ? 29 THR A C 1 ATOM 227 O O . THR A 1 30 ? 22.701 0.053 38.658 1.00 45.37 ? 29 THR A O 1 ATOM 228 C CB . THR A 1 30 ? 21.522 2.762 37.372 1.00 37.43 ? 29 THR A CB 1 ATOM 229 O OG1 . THR A 1 30 ? 20.694 1.624 37.098 1.00 36.07 ? 29 THR A OG1 1 ATOM 230 C CG2 . THR A 1 30 ? 21.751 3.482 36.112 1.00 37.20 ? 29 THR A CG2 1 ATOM 231 N N . GLN A 1 31 ? 23.870 0.467 36.786 1.00 26.90 ? 30 GLN A N 1 ATOM 232 C CA . GLN A 1 31 ? 24.366 -0.900 36.624 1.00 29.99 ? 30 GLN A CA 1 ATOM 233 C C . GLN A 1 31 ? 25.278 -0.956 35.408 1.00 31.56 ? 30 GLN A C 1 ATOM 234 O O . GLN A 1 31 ? 25.188 -0.128 34.497 1.00 27.85 ? 30 GLN A O 1 ATOM 235 C CB . GLN A 1 31 ? 23.241 -1.938 36.480 1.00 31.55 ? 30 GLN A CB 1 ATOM 236 C CG . GLN A 1 31 ? 22.722 -2.184 35.058 1.00 29.98 ? 30 GLN A CG 1 ATOM 237 C CD . GLN A 1 31 ? 21.415 -2.979 35.050 1.00 31.73 ? 30 GLN A CD 1 ATOM 238 O OE1 . GLN A 1 31 ? 20.705 -3.016 36.055 1.00 30.22 ? 30 GLN A OE1 1 ATOM 239 N NE2 . GLN A 1 31 ? 21.094 -3.617 33.917 1.00 24.14 ? 30 GLN A NE2 1 ATOM 240 N N . ILE A 1 32 ? 26.168 -1.948 35.413 1.00 28.84 ? 31 ILE A N 1 ATOM 241 C CA . ILE A 1 32 ? 27.160 -2.125 34.363 1.00 28.53 ? 31 ILE A CA 1 ATOM 242 C C . ILE A 1 32 ? 27.084 -3.566 33.898 1.00 34.39 ? 31 ILE A C 1 ATOM 243 O O . ILE A 1 32 ? 26.666 -4.456 34.641 1.00 36.94 ? 31 ILE A O 1 ATOM 244 C CB . ILE A 1 32 ? 28.568 -1.802 34.857 1.00 27.99 ? 31 ILE A CB 1 ATOM 245 C CG1 . ILE A 1 32 ? 29.005 -2.893 35.845 1.00 31.15 ? 31 ILE A CG1 1 ATOM 246 C CG2 . ILE A 1 32 ? 28.549 -0.456 35.527 1.00 40.09 ? 31 ILE A CG2 1 ATOM 247 C CD1 . ILE A 1 32 ? 30.332 -2.661 36.544 1.00 37.36 ? 31 ILE A CD1 1 ATOM 248 N N . SER A 1 33 ? 27.510 -3.805 32.663 1.00 34.09 ? 32 SER A N 1 ATOM 249 C CA . SER A 1 33 ? 27.271 -5.121 32.106 1.00 23.01 ? 32 SER A CA 1 ATOM 250 C C . SER A 1 33 ? 28.163 -5.335 30.900 1.00 28.08 ? 32 SER A C 1 ATOM 251 O O . SER A 1 33 ? 28.614 -4.384 30.256 1.00 31.69 ? 32 SER A O 1 ATOM 252 C CB . SER A 1 33 ? 25.809 -5.284 31.707 1.00 24.30 ? 32 SER A CB 1 ATOM 253 O OG . SER A 1 33 ? 25.655 -4.930 30.355 1.00 32.01 ? 32 SER A OG 1 ATOM 254 N N . TRP A 1 34 ? 28.438 -6.606 30.624 1.00 27.89 ? 33 TRP A N 1 ATOM 255 C CA . TRP A 1 34 ? 29.042 -7.046 29.376 1.00 23.09 ? 33 TRP A CA 1 ATOM 256 C C . TRP A 1 34 ? 27.965 -7.783 28.595 1.00 25.87 ? 33 TRP A C 1 ATOM 257 O O . TRP A 1 34 ? 27.163 -8.519 29.175 1.00 26.93 ? 33 TRP A O 1 ATOM 258 C CB . TRP A 1 34 ? 30.250 -7.956 29.613 1.00 19.19 ? 33 TRP A CB 1 ATOM 259 C CG . TRP A 1 34 ? 31.637 -7.267 29.793 1.00 33.40 ? 33 TRP A CG 1 ATOM 260 C CD1 . TRP A 1 34 ? 32.306 -7.056 30.970 1.00 28.42 ? 33 TRP A CD1 1 ATOM 261 C CD2 . TRP A 1 34 ? 32.503 -6.757 28.755 1.00 26.48 ? 33 TRP A CD2 1 ATOM 262 N NE1 . TRP A 1 34 ? 33.518 -6.447 30.728 1.00 30.12 ? 33 TRP A NE1 1 ATOM 263 C CE2 . TRP A 1 34 ? 33.655 -6.240 29.384 1.00 24.46 ? 33 TRP A CE2 1 ATOM 264 C CE3 . TRP A 1 34 ? 32.401 -6.674 27.361 1.00 29.05 ? 33 TRP A CE3 1 ATOM 265 C CZ2 . TRP A 1 34 ? 34.704 -5.672 28.674 1.00 25.78 ? 33 TRP A CZ2 1 ATOM 266 C CZ3 . TRP A 1 34 ? 33.427 -6.095 26.655 1.00 27.66 ? 33 TRP A CZ3 1 ATOM 267 C CH2 . TRP A 1 34 ? 34.575 -5.598 27.317 1.00 32.71 ? 33 TRP A CH2 1 ATOM 268 N N . GLU A 1 35 ? 27.906 -7.551 27.294 1.00 23.89 ? 34 GLU A N 1 ATOM 269 C CA . GLU A 1 35 ? 26.889 -8.177 26.476 1.00 29.00 ? 34 GLU A CA 1 ATOM 270 C C . GLU A 1 35 ? 27.520 -8.741 25.213 1.00 27.53 ? 34 GLU A C 1 ATOM 271 O O . GLU A 1 35 ? 28.566 -8.276 24.758 1.00 32.45 ? 34 GLU A O 1 ATOM 272 C CB . GLU A 1 35 ? 25.737 -7.191 26.152 1.00 33.53 ? 34 GLU A CB 1 ATOM 273 C CG . GLU A 1 35 ? 25.035 -6.658 27.416 1.00 36.34 ? 34 GLU A CG 1 ATOM 274 C CD . GLU A 1 35 ? 23.773 -5.849 27.129 1.00 55.17 ? 34 GLU A CD 1 ATOM 275 O OE1 . GLU A 1 35 ? 23.437 -5.646 25.938 1.00 55.56 ? 34 GLU A OE1 1 ATOM 276 O OE2 . GLU A 1 35 ? 23.112 -5.417 28.106 1.00 57.85 ? 34 GLU A OE2 1 ATOM 277 N N . LYS A 1 36 ? 26.888 -9.771 24.667 1.00 30.68 ? 35 LYS A N 1 ATOM 278 C CA . LYS A 1 36 ? 27.351 -10.432 23.456 1.00 37.68 ? 35 LYS A CA 1 ATOM 279 C C . LYS A 1 36 ? 26.369 -10.182 22.321 1.00 44.04 ? 35 LYS A C 1 ATOM 280 O O . LYS A 1 36 ? 25.162 -10.408 22.470 1.00 51.09 ? 35 LYS A O 1 ATOM 281 C CB . LYS A 1 36 ? 27.513 -11.933 23.681 1.00 40.40 ? 35 LYS A CB 1 ATOM 282 C CG . LYS A 1 36 ? 28.072 -12.664 22.498 1.00 40.37 ? 35 LYS A CG 1 ATOM 283 C CD . LYS A 1 36 ? 29.550 -12.464 22.379 1.00 34.17 ? 35 LYS A CD 1 ATOM 284 C CE . LYS A 1 36 ? 30.080 -13.345 21.270 1.00 38.48 ? 35 LYS A CE 1 ATOM 285 N NZ . LYS A 1 36 ? 29.751 -14.767 21.525 1.00 35.64 ? 35 LYS A NZ 1 ATOM 286 N N . ILE A 1 37 ? 26.894 -9.748 21.183 1.00 45.52 ? 36 ILE A N 1 ATOM 287 C CA . ILE A 1 37 ? 26.056 -9.415 20.041 1.00 47.03 ? 36 ILE A CA 1 ATOM 288 C C . ILE A 1 37 ? 25.571 -10.691 19.371 1.00 51.64 ? 36 ILE A C 1 ATOM 289 O O . ILE A 1 37 ? 26.374 -11.541 18.974 1.00 53.56 ? 36 ILE A O 1 ATOM 290 C CB . ILE A 1 37 ? 26.823 -8.550 19.046 1.00 45.49 ? 36 ILE A CB 1 ATOM 291 C CG1 . ILE A 1 37 ? 26.965 -7.135 19.604 1.00 37.94 ? 36 ILE A CG1 1 ATOM 292 C CG2 . ILE A 1 37 ? 26.136 -8.612 17.704 1.00 45.31 ? 36 ILE A CG2 1 ATOM 293 C CD1 . ILE A 1 37 ? 27.694 -6.230 18.696 1.00 39.19 ? 36 ILE A CD1 1 ATOM 294 N N . HIS A 1 38 ? 24.253 -10.810 19.217 1.00 63.85 ? 37 HIS A N 1 ATOM 295 C CA . HIS A 1 38 ? 23.615 -11.956 18.569 1.00 60.33 ? 37 HIS A CA 1 ATOM 296 C C . HIS A 1 38 ? 22.560 -11.466 17.588 1.00 73.44 ? 37 HIS A C 1 ATOM 297 O O . HIS A 1 38 ? 21.431 -11.151 17.980 1.00 79.62 ? 37 HIS A O 1 ATOM 298 C CB . HIS A 1 38 ? 23.016 -12.892 19.592 1.00 60.35 ? 37 HIS A CB 1 ATOM 299 C CG . HIS A 1 38 ? 24.035 -13.755 20.238 1.00 71.32 ? 37 HIS A CG 1 ATOM 300 N ND1 . HIS A 1 38 ? 23.986 -14.126 21.564 1.00 70.97 ? 37 HIS A ND1 1 ATOM 301 C CD2 . HIS A 1 38 ? 25.171 -14.290 19.733 1.00 72.83 ? 37 HIS A CD2 1 ATOM 302 C CE1 . HIS A 1 38 ? 25.037 -14.880 21.837 1.00 67.58 ? 37 HIS A CE1 1 ATOM 303 N NE2 . HIS A 1 38 ? 25.775 -14.990 20.748 1.00 71.34 ? 37 HIS A NE2 1 ATOM 304 N N . GLY A 1 39 ? 22.919 -11.465 16.312 1.00 75.53 ? 38 GLY A N 1 ATOM 305 C CA . GLY A 1 39 ? 22.098 -10.785 15.331 1.00 76.59 ? 38 GLY A CA 1 ATOM 306 C C . GLY A 1 39 ? 22.238 -9.295 15.553 1.00 74.23 ? 38 GLY A C 1 ATOM 307 O O . GLY A 1 39 ? 23.342 -8.769 15.709 1.00 68.36 ? 38 GLY A O 1 ATOM 308 N N . LYS A 1 40 ? 21.113 -8.591 15.580 1.00 82.27 ? 39 LYS A N 1 ATOM 309 C CA . LYS A 1 40 ? 21.160 -7.204 16.014 1.00 86.90 ? 39 LYS A CA 1 ATOM 310 C C . LYS A 1 40 ? 20.857 -7.049 17.499 1.00 84.71 ? 39 LYS A C 1 ATOM 311 O O . LYS A 1 40 ? 21.241 -6.032 18.092 1.00 83.11 ? 39 LYS A O 1 ATOM 312 C CB . LYS A 1 40 ? 20.195 -6.340 15.183 1.00 88.74 ? 39 LYS A CB 1 ATOM 313 C CG . LYS A 1 40 ? 20.493 -4.839 15.275 1.00 83.75 ? 39 LYS A CG 1 ATOM 314 C CD . LYS A 1 40 ? 20.173 -4.087 13.979 1.00 86.72 ? 39 LYS A CD 1 ATOM 315 C CE . LYS A 1 40 ? 20.721 -4.787 12.733 1.00 80.29 ? 39 LYS A CE 1 ATOM 316 N NZ . LYS A 1 40 ? 22.213 -4.777 12.665 1.00 83.78 ? 39 LYS A NZ 1 ATOM 317 N N . SER A 1 41 ? 20.213 -8.041 18.118 1.00 77.33 ? 40 SER A N 1 ATOM 318 C CA . SER A 1 41 ? 20.016 -8.020 19.558 1.00 72.22 ? 40 SER A CA 1 ATOM 319 C C . SER A 1 41 ? 21.294 -8.460 20.272 1.00 67.73 ? 40 SER A C 1 ATOM 320 O O . SER A 1 41 ? 22.219 -9.020 19.679 1.00 59.17 ? 40 SER A O 1 ATOM 321 C CB . SER A 1 41 ? 18.852 -8.925 19.970 1.00 72.63 ? 40 SER A CB 1 ATOM 322 O OG . SER A 1 41 ? 19.119 -10.286 19.659 1.00 71.99 ? 40 SER A OG 1 ATOM 323 N N . THR A 1 42 ? 21.335 -8.197 21.568 1.00 62.26 ? 41 THR A N 1 ATOM 324 C CA . THR A 1 42 ? 22.464 -8.594 22.379 1.00 53.34 ? 41 THR A CA 1 ATOM 325 C C . THR A 1 42 ? 22.013 -9.535 23.487 1.00 51.37 ? 41 THR A C 1 ATOM 326 O O . THR A 1 42 ? 20.917 -9.401 24.033 1.00 55.42 ? 41 THR A O 1 ATOM 327 C CB . THR A 1 42 ? 23.175 -7.387 22.994 1.00 53.94 ? 41 THR A CB 1 ATOM 328 O OG1 . THR A 1 42 ? 22.361 -6.826 24.033 1.00 58.10 ? 41 THR A OG1 1 ATOM 329 C CG2 . THR A 1 42 ? 23.464 -6.344 21.940 1.00 52.13 ? 41 THR A CG2 1 ATOM 330 N N . GLN A 1 43 ? 22.870 -10.496 23.793 1.00 47.12 ? 42 GLN A N 1 ATOM 331 C CA . GLN A 1 43 ? 22.724 -11.378 24.935 1.00 46.76 ? 42 GLN A CA 1 ATOM 332 C C . GLN A 1 43 ? 23.571 -10.847 26.087 1.00 38.34 ? 42 GLN A C 1 ATOM 333 O O . GLN A 1 43 ? 24.730 -10.491 25.892 1.00 39.68 ? 42 GLN A O 1 ATOM 334 C CB . GLN A 1 43 ? 23.197 -12.796 24.586 1.00 53.97 ? 42 GLN A CB 1 ATOM 335 C CG . GLN A 1 43 ? 23.971 -13.453 25.768 1.00 65.15 ? 42 GLN A CG 1 ATOM 336 C CD . GLN A 1 43 ? 24.592 -14.834 25.490 1.00 72.92 ? 42 GLN A CD 1 ATOM 337 O OE1 . GLN A 1 43 ? 25.197 -15.086 24.446 1.00 81.03 ? 42 GLN A OE1 1 ATOM 338 N NE2 . GLN A 1 43 ? 24.442 -15.734 26.449 1.00 71.71 ? 42 GLN A NE2 1 ATOM 339 N N . THR A 1 44 ? 23.003 -10.818 27.290 1.00 38.42 ? 43 THR A N 1 ATOM 340 C CA . THR A 1 44 ? 23.802 -10.466 28.458 1.00 33.79 ? 43 THR A CA 1 ATOM 341 C C . THR A 1 44 ? 24.813 -11.566 28.790 1.00 36.59 ? 43 THR A C 1 ATOM 342 O O . THR A 1 44 ? 24.496 -12.755 28.775 1.00 34.27 ? 43 THR A O 1 ATOM 343 C CB . THR A 1 44 ? 22.928 -10.228 29.689 1.00 34.72 ? 43 THR A CB 1 ATOM 344 O OG1 . THR A 1 44 ? 21.877 -9.299 29.400 1.00 39.20 ? 43 THR A OG1 1 ATOM 345 C CG2 . THR A 1 44 ? 23.777 -9.652 30.784 1.00 27.58 ? 43 THR A CG2 1 ATOM 346 N N . VAL A 1 45 ? 26.047 -11.154 29.097 1.00 30.92 ? 44 VAL A N 1 ATOM 347 C CA . VAL A 1 45 ? 27.090 -12.050 29.580 1.00 23.15 ? 44 VAL A CA 1 ATOM 348 C C . VAL A 1 45 ? 27.141 -11.925 31.097 1.00 25.68 ? 44 VAL A C 1 ATOM 349 O O . VAL A 1 45 ? 26.938 -12.918 31.811 1.00 26.45 ? 44 VAL A O 1 ATOM 350 C CB . VAL A 1 45 ? 28.447 -11.732 28.923 1.00 28.20 ? 44 VAL A CB 1 ATOM 351 C CG1 . VAL A 1 45 ? 29.534 -12.663 29.439 1.00 24.20 ? 44 VAL A CG1 1 ATOM 352 C CG2 . VAL A 1 45 ? 28.334 -11.856 27.405 1.00 25.79 ? 44 VAL A CG2 1 ATOM 353 N N . ALA A 1 46 ? 27.352 -10.701 31.603 1.00 17.40 ? 45 ALA A N 1 ATOM 354 C CA . ALA A 1 46 ? 27.476 -10.484 33.041 1.00 18.77 ? 45 ALA A CA 1 ATOM 355 C C . ALA A 1 46 ? 27.020 -9.083 33.406 1.00 25.29 ? 45 ALA A C 1 ATOM 356 O O . ALA A 1 46 ? 27.189 -8.141 32.629 1.00 27.88 ? 45 ALA A O 1 ATOM 357 C CB . ALA A 1 46 ? 28.920 -10.705 33.531 1.00 29.01 ? 45 ALA A CB 1 ATOM 358 N N . VAL A 1 47 ? 26.432 -8.961 34.603 1.00 27.11 ? 46 VAL A N 1 ATOM 359 C CA . VAL A 1 47 ? 25.794 -7.735 35.073 1.00 25.94 ? 46 VAL A CA 1 ATOM 360 C C . VAL A 1 47 ? 26.160 -7.525 36.522 1.00 31.50 ? 46 VAL A C 1 ATOM 361 O O . VAL A 1 47 ? 26.039 -8.442 37.343 1.00 29.84 ? 46 VAL A O 1 ATOM 362 C CB . VAL A 1 47 ? 24.255 -7.744 35.009 1.00 24.50 ? 46 VAL A CB 1 ATOM 363 C CG1 . VAL A 1 47 ? 23.758 -6.320 34.984 1.00 20.78 ? 46 VAL A CG1 1 ATOM 364 C CG2 . VAL A 1 47 ? 23.758 -8.537 33.884 1.00 25.63 ? 46 VAL A CG2 1 ATOM 365 N N . HIS A 1 48 ? 26.504 -6.290 36.845 1.00 22.63 ? 47 HIS A N 1 ATOM 366 C CA . HIS A 1 48 ? 26.835 -5.890 38.194 1.00 26.42 ? 47 HIS A CA 1 ATOM 367 C C . HIS A 1 48 ? 25.893 -4.749 38.549 1.00 28.74 ? 47 HIS A C 1 ATOM 368 O O . HIS A 1 48 ? 25.855 -3.722 37.858 1.00 31.95 ? 47 HIS A O 1 ATOM 369 C CB . HIS A 1 48 ? 28.319 -5.494 38.280 1.00 25.12 ? 47 HIS A CB 1 ATOM 370 C CG . HIS A 1 48 ? 28.772 -5.063 39.639 1.00 24.87 ? 47 HIS A CG 1 ATOM 371 N ND1 . HIS A 1 48 ? 28.035 -5.291 40.782 1.00 32.87 ? 47 HIS A ND1 1 ATOM 372 C CD2 . HIS A 1 48 ? 29.868 -4.374 40.030 1.00 27.53 ? 47 HIS A CD2 1 ATOM 373 C CE1 . HIS A 1 48 ? 28.670 -4.783 41.822 1.00 27.67 ? 47 HIS A CE1 1 ATOM 374 N NE2 . HIS A 1 48 ? 29.787 -4.227 41.392 1.00 32.44 ? 47 HIS A NE2 1 ATOM 375 N N . HIS A 1 49 ? 25.105 -4.952 39.589 1.00 27.97 ? 48 HIS A N 1 ATOM 376 C CA . HIS A 1 49 ? 24.191 -3.963 40.103 1.00 31.26 ? 48 HIS A CA 1 ATOM 377 C C . HIS A 1 49 ? 24.537 -3.666 41.558 1.00 35.01 ? 48 HIS A C 1 ATOM 378 O O . HIS A 1 49 ? 24.860 -4.586 42.318 1.00 31.37 ? 48 HIS A O 1 ATOM 379 C CB . HIS A 1 49 ? 22.764 -4.471 39.986 1.00 24.17 ? 48 HIS A CB 1 ATOM 380 C CG . HIS A 1 49 ? 21.706 -3.437 40.222 1.00 37.20 ? 48 HIS A CG 1 ATOM 381 N ND1 . HIS A 1 49 ? 21.257 -3.103 41.484 1.00 38.19 ? 48 HIS A ND1 1 ATOM 382 C CD2 . HIS A 1 49 ? 20.954 -2.720 39.355 1.00 29.79 ? 48 HIS A CD2 1 ATOM 383 C CE1 . HIS A 1 49 ? 20.295 -2.206 41.383 1.00 27.94 ? 48 HIS A CE1 1 ATOM 384 N NE2 . HIS A 1 49 ? 20.084 -1.967 40.101 1.00 28.91 ? 48 HIS A NE2 1 ATOM 385 N N . PRO A 1 50 ? 24.505 -2.393 41.962 1.00 34.91 ? 49 PRO A N 1 ATOM 386 C CA . PRO A 1 50 ? 24.954 -2.028 43.320 1.00 32.67 ? 49 PRO A CA 1 ATOM 387 C C . PRO A 1 50 ? 24.171 -2.676 44.438 1.00 34.30 ? 49 PRO A C 1 ATOM 388 O O . PRO A 1 50 ? 24.752 -2.966 45.491 1.00 44.04 ? 49 PRO A O 1 ATOM 389 C CB . PRO A 1 50 ? 24.779 -0.503 43.342 1.00 35.63 ? 49 PRO A CB 1 ATOM 390 C CG . PRO A 1 50 ? 23.738 -0.230 42.291 1.00 34.39 ? 49 PRO A CG 1 ATOM 391 C CD . PRO A 1 50 ? 24.045 -1.223 41.202 1.00 35.81 ? 49 PRO A CD 1 ATOM 392 N N . GLN A 1 51 ? 22.865 -2.883 44.264 1.00 37.97 ? 50 GLN A N 1 ATOM 393 C CA . GLN A 1 51 ? 22.044 -3.553 45.265 1.00 32.14 ? 50 GLN A CA 1 ATOM 394 C C . GLN A 1 51 ? 21.797 -5.027 44.962 1.00 37.02 ? 50 GLN A C 1 ATOM 395 O O . GLN A 1 51 ? 21.716 -5.838 45.889 1.00 34.90 ? 50 GLN A O 1 ATOM 396 C CB . GLN A 1 51 ? 20.695 -2.848 45.401 1.00 37.79 ? 50 GLN A CB 1 ATOM 397 C CG . GLN A 1 51 ? 20.800 -1.352 45.675 1.00 48.32 ? 50 GLN A CG 1 ATOM 398 C CD . GLN A 1 51 ? 21.706 -1.014 46.868 1.00 56.33 ? 50 GLN A CD 1 ATOM 399 O OE1 . GLN A 1 51 ? 22.555 -0.126 46.771 1.00 51.53 ? 50 GLN A OE1 1 ATOM 400 N NE2 . GLN A 1 51 ? 21.518 -1.714 47.996 1.00 50.86 ? 50 GLN A NE2 1 ATOM 401 N N . TYR A 1 52 ? 21.697 -5.406 43.697 1.00 31.39 ? 51 TYR A N 1 ATOM 402 C CA . TYR A 1 52 ? 21.309 -6.762 43.351 1.00 26.68 ? 51 TYR A CA 1 ATOM 403 C C . TYR A 1 52 ? 22.472 -7.742 43.195 1.00 30.57 ? 51 TYR A C 1 ATOM 404 O O . TYR A 1 52 ? 22.235 -8.953 43.234 1.00 31.98 ? 51 TYR A O 1 ATOM 405 C CB . TYR A 1 52 ? 20.490 -6.717 42.070 1.00 31.13 ? 51 TYR A CB 1 ATOM 406 C CG . TYR A 1 52 ? 19.222 -5.928 42.250 1.00 35.62 ? 51 TYR A CG 1 ATOM 407 C CD1 . TYR A 1 52 ? 18.530 -5.978 43.449 1.00 34.75 ? 51 TYR A CD1 1 ATOM 408 C CD2 . TYR A 1 52 ? 18.715 -5.134 41.229 1.00 38.24 ? 51 TYR A CD2 1 ATOM 409 C CE1 . TYR A 1 52 ? 17.375 -5.276 43.628 1.00 41.02 ? 51 TYR A CE1 1 ATOM 410 C CE2 . TYR A 1 52 ? 17.555 -4.417 41.404 1.00 33.78 ? 51 TYR A CE2 1 ATOM 411 C CZ . TYR A 1 52 ? 16.886 -4.503 42.607 1.00 42.16 ? 51 TYR A CZ 1 ATOM 412 O OH . TYR A 1 52 ? 15.716 -3.811 42.806 1.00 64.80 ? 51 TYR A OH 1 ATOM 413 N N . GLY A 1 53 ? 23.701 -7.263 42.999 1.00 30.76 ? 52 GLY A N 1 ATOM 414 C CA . GLY A 1 53 ? 24.865 -8.128 42.911 1.00 30.72 ? 52 GLY A CA 1 ATOM 415 C C . GLY A 1 53 ? 25.257 -8.520 41.497 1.00 35.37 ? 52 GLY A C 1 ATOM 416 O O . GLY A 1 53 ? 24.724 -8.032 40.498 1.00 34.04 ? 52 GLY A O 1 ATOM 417 N N . PHE A 1 54 ? 26.220 -9.441 41.424 1.00 30.95 ? 53 PHE A N 1 ATOM 418 C CA . PHE A 1 54 ? 26.666 -9.965 40.148 1.00 29.39 ? 53 PHE A CA 1 ATOM 419 C C . PHE A 1 54 ? 25.659 -10.956 39.592 1.00 27.29 ? 53 PHE A C 1 ATOM 420 O O . PHE A 1 54 ? 24.888 -11.577 40.320 1.00 29.86 ? 53 PHE A O 1 ATOM 421 C CB . PHE A 1 54 ? 28.007 -10.677 40.271 1.00 33.02 ? 53 PHE A CB 1 ATOM 422 C CG . PHE A 1 54 ? 29.099 -9.829 40.831 1.00 34.91 ? 53 PHE A CG 1 ATOM 423 C CD1 . PHE A 1 54 ? 29.189 -8.492 40.514 1.00 37.87 ? 53 PHE A CD1 1 ATOM 424 C CD2 . PHE A 1 54 ? 30.040 -10.377 41.695 1.00 39.52 ? 53 PHE A CD2 1 ATOM 425 C CE1 . PHE A 1 54 ? 30.187 -7.718 41.037 1.00 32.69 ? 53 PHE A CE1 1 ATOM 426 C CE2 . PHE A 1 54 ? 31.042 -9.599 42.215 1.00 42.65 ? 53 PHE A CE2 1 ATOM 427 C CZ . PHE A 1 54 ? 31.104 -8.262 41.886 1.00 41.54 ? 53 PHE A CZ 1 ATOM 428 N N . SER A 1 55 ? 25.691 -11.121 38.276 1.00 26.76 ? 54 SER A N 1 ATOM 429 C CA . SER A 1 55 ? 24.883 -12.147 37.643 1.00 23.03 ? 54 SER A CA 1 ATOM 430 C C . SER A 1 55 ? 25.547 -12.522 36.336 1.00 24.44 ? 54 SER A C 1 ATOM 431 O O . SER A 1 55 ? 26.055 -11.651 35.627 1.00 24.30 ? 54 SER A O 1 ATOM 432 C CB . SER A 1 55 ? 23.443 -11.683 37.415 1.00 27.46 ? 54 SER A CB 1 ATOM 433 O OG . SER A 1 55 ? 22.737 -12.613 36.601 1.00 34.20 ? 54 SER A OG 1 ATOM 434 N N . VAL A 1 56 ? 25.567 -13.829 36.050 1.00 25.53 ? 55 VAL A N 1 ATOM 435 C CA . VAL A 1 56 ? 26.185 -14.398 34.856 1.00 25.53 ? 55 VAL A CA 1 ATOM 436 C C . VAL A 1 56 ? 25.147 -15.233 34.123 1.00 20.82 ? 55 VAL A C 1 ATOM 437 O O . VAL A 1 56 ? 24.294 -15.867 34.744 1.00 23.89 ? 55 VAL A O 1 ATOM 438 C CB . VAL A 1 56 ? 27.424 -15.245 35.207 1.00 22.35 ? 55 VAL A CB 1 ATOM 439 C CG1 . VAL A 1 56 ? 28.136 -15.728 33.934 1.00 21.10 ? 55 VAL A CG1 1 ATOM 440 C CG2 . VAL A 1 56 ? 28.342 -14.443 36.068 1.00 14.51 ? 55 VAL A CG2 1 ATOM 441 N N . GLN A 1 57 ? 25.215 -15.232 32.803 1.00 25.94 ? 56 GLN A N 1 ATOM 442 C CA . GLN A 1 57 ? 24.101 -15.701 32.001 1.00 19.83 ? 56 GLN A CA 1 ATOM 443 C C . GLN A 1 57 ? 24.571 -16.699 30.970 1.00 22.59 ? 56 GLN A C 1 ATOM 444 O O . GLN A 1 57 ? 25.731 -16.687 30.537 1.00 30.10 ? 56 GLN A O 1 ATOM 445 C CB . GLN A 1 57 ? 23.397 -14.525 31.299 1.00 22.23 ? 56 GLN A CB 1 ATOM 446 C CG . GLN A 1 57 ? 22.192 -13.975 32.072 1.00 22.40 ? 56 GLN A CG 1 ATOM 447 C CD . GLN A 1 57 ? 22.444 -13.869 33.537 1.00 31.11 ? 56 GLN A CD 1 ATOM 448 O OE1 . GLN A 1 57 ? 23.337 -13.143 33.977 1.00 45.57 ? 56 GLN A OE1 1 ATOM 449 N NE2 . GLN A 1 57 ? 21.637 -14.573 34.322 1.00 37.81 ? 56 GLN A NE2 1 ATOM 450 N N . GLY A 1 58 ? 23.636 -17.547 30.559 1.00 26.31 ? 57 GLY A N 1 ATOM 451 C CA . GLY A 1 58 ? 23.861 -18.430 29.433 1.00 19.07 ? 57 GLY A CA 1 ATOM 452 C C . GLY A 1 58 ? 24.925 -19.447 29.768 1.00 24.87 ? 57 GLY A C 1 ATOM 453 O O . GLY A 1 58 ? 25.066 -19.878 30.911 1.00 29.05 ? 57 GLY A O 1 ATOM 454 N N . ASP A 1 59 ? 25.711 -19.805 28.752 1.00 25.50 ? 58 ASP A N 1 ATOM 455 C CA . ASP A 1 59 ? 26.817 -20.734 28.905 1.00 27.98 ? 58 ASP A CA 1 ATOM 456 C C . ASP A 1 59 ? 28.066 -20.074 29.493 1.00 32.38 ? 58 ASP A C 1 ATOM 457 O O . ASP A 1 59 ? 29.134 -20.703 29.537 1.00 31.67 ? 58 ASP A O 1 ATOM 458 C CB . ASP A 1 59 ? 27.145 -21.379 27.558 1.00 36.38 ? 58 ASP A CB 1 ATOM 459 C CG . ASP A 1 59 ? 27.791 -20.410 26.594 1.00 45.17 ? 58 ASP A CG 1 ATOM 460 O OD1 . ASP A 1 59 ? 27.566 -19.192 26.746 1.00 45.10 ? 58 ASP A OD1 1 ATOM 461 O OD2 . ASP A 1 59 ? 28.514 -20.871 25.682 1.00 47.99 ? 58 ASP A OD2 1 ATOM 462 N N . TYR A 1 60 ? 27.963 -18.827 29.936 1.00 24.97 ? 59 TYR A N 1 ATOM 463 C CA . TYR A 1 60 ? 29.064 -18.207 30.646 1.00 22.51 ? 59 TYR A CA 1 ATOM 464 C C . TYR A 1 60 ? 29.102 -18.595 32.123 1.00 24.48 ? 59 TYR A C 1 ATOM 465 O O . TYR A 1 60 ? 30.139 -18.404 32.760 1.00 26.57 ? 59 TYR A O 1 ATOM 466 C CB . TYR A 1 60 ? 28.979 -16.685 30.480 1.00 22.54 ? 59 TYR A CB 1 ATOM 467 C CG . TYR A 1 60 ? 29.245 -16.275 29.063 1.00 22.18 ? 59 TYR A CG 1 ATOM 468 C CD1 . TYR A 1 60 ? 30.534 -16.158 28.603 1.00 20.61 ? 59 TYR A CD1 1 ATOM 469 C CD2 . TYR A 1 60 ? 28.204 -16.062 28.165 1.00 23.07 ? 59 TYR A CD2 1 ATOM 470 C CE1 . TYR A 1 60 ? 30.801 -15.807 27.296 1.00 26.25 ? 59 TYR A CE1 1 ATOM 471 C CE2 . TYR A 1 60 ? 28.456 -15.721 26.853 1.00 22.71 ? 59 TYR A CE2 1 ATOM 472 C CZ . TYR A 1 60 ? 29.766 -15.587 26.421 1.00 27.22 ? 59 TYR A CZ 1 ATOM 473 O OH . TYR A 1 60 ? 30.061 -15.225 25.121 1.00 28.89 ? 59 TYR A OH 1 ATOM 474 N N . GLN A 1 61 ? 28.016 -19.149 32.673 1.00 19.77 ? 60 GLN A N 1 ATOM 475 C CA . GLN A 1 61 ? 27.983 -19.508 34.087 1.00 21.32 ? 60 GLN A CA 1 ATOM 476 C C . GLN A 1 61 ? 29.079 -20.513 34.450 1.00 29.68 ? 60 GLN A C 1 ATOM 477 O O . GLN A 1 61 ? 29.318 -21.495 33.744 1.00 30.69 ? 60 GLN A O 1 ATOM 478 C CB . GLN A 1 61 ? 26.624 -20.088 34.459 1.00 17.83 ? 60 GLN A CB 1 ATOM 479 C CG . GLN A 1 61 ? 25.464 -19.212 34.124 1.00 15.12 ? 60 GLN A CG 1 ATOM 480 C CD . GLN A 1 61 ? 24.204 -19.618 34.882 1.00 23.79 ? 60 GLN A CD 1 ATOM 481 O OE1 . GLN A 1 61 ? 23.219 -20.040 34.273 1.00 26.71 ? 60 GLN A OE1 1 ATOM 482 N NE2 . GLN A 1 61 ? 24.240 -19.517 36.225 1.00 15.63 ? 60 GLN A NE2 1 ATOM 483 N N . GLY A 1 62 ? 29.721 -20.282 35.589 1.00 29.09 ? 61 GLY A N 1 ATOM 484 C CA . GLY A 1 62 ? 30.863 -21.058 35.984 1.00 20.94 ? 61 GLY A CA 1 ATOM 485 C C . GLY A 1 62 ? 32.113 -20.778 35.192 1.00 27.55 ? 61 GLY A C 1 ATOM 486 O O . GLY A 1 62 ? 33.143 -21.406 35.459 1.00 30.67 ? 61 GLY A O 1 ATOM 487 N N . ARG A 1 63 ? 32.062 -19.861 34.225 1.00 23.02 ? 62 ARG A N 1 ATOM 488 C CA . ARG A 1 63 ? 33.227 -19.509 33.429 1.00 25.02 ? 62 ARG A CA 1 ATOM 489 C C . ARG A 1 63 ? 33.581 -18.028 33.481 1.00 28.88 ? 62 ARG A C 1 ATOM 490 O O . ARG A 1 63 ? 34.536 -17.607 32.807 1.00 25.90 ? 62 ARG A O 1 ATOM 491 C CB . ARG A 1 63 ? 32.999 -19.937 31.980 1.00 19.60 ? 62 ARG A CB 1 ATOM 492 C CG . ARG A 1 63 ? 32.586 -21.382 31.903 1.00 24.95 ? 62 ARG A CG 1 ATOM 493 C CD . ARG A 1 63 ? 32.156 -21.766 30.524 1.00 24.25 ? 62 ARG A CD 1 ATOM 494 N NE . ARG A 1 63 ? 33.092 -21.231 29.579 1.00 29.78 ? 62 ARG A NE 1 ATOM 495 C CZ . ARG A 1 63 ? 32.785 -20.404 28.604 1.00 27.40 ? 62 ARG A CZ 1 ATOM 496 N NH1 . ARG A 1 63 ? 31.529 -20.042 28.405 1.00 29.60 ? 62 ARG A NH1 1 ATOM 497 N NH2 . ARG A 1 63 ? 33.749 -19.972 27.810 1.00 30.45 ? 62 ARG A NH2 1 ATOM 498 N N . VAL A 1 64 ? 32.858 -17.230 34.263 1.00 21.44 ? 63 VAL A N 1 ATOM 499 C CA . VAL A 1 64 ? 33.049 -15.788 34.294 1.00 26.28 ? 63 VAL A CA 1 ATOM 500 C C . VAL A 1 64 ? 33.249 -15.348 35.734 1.00 31.56 ? 63 VAL A C 1 ATOM 501 O O . VAL A 1 64 ? 32.522 -15.790 36.628 1.00 28.45 ? 63 VAL A O 1 ATOM 502 C CB . VAL A 1 64 ? 31.852 -15.032 33.676 1.00 21.43 ? 63 VAL A CB 1 ATOM 503 C CG1 . VAL A 1 64 ? 31.979 -13.586 33.952 1.00 18.13 ? 63 VAL A CG1 1 ATOM 504 C CG2 . VAL A 1 64 ? 31.778 -15.260 32.180 1.00 22.88 ? 63 VAL A CG2 1 ATOM 505 N N . LEU A 1 65 ? 34.216 -14.460 35.951 1.00 26.99 ? 64 LEU A N 1 ATOM 506 C CA . LEU A 1 65 ? 34.452 -13.850 37.247 1.00 27.35 ? 64 LEU A CA 1 ATOM 507 C C . LEU A 1 65 ? 34.534 -12.346 37.062 1.00 29.87 ? 64 LEU A C 1 ATOM 508 O O . LEU A 1 65 ? 35.137 -11.859 36.096 1.00 25.70 ? 64 LEU A O 1 ATOM 509 C CB . LEU A 1 65 ? 35.768 -14.347 37.884 1.00 32.41 ? 64 LEU A CB 1 ATOM 510 C CG . LEU A 1 65 ? 35.985 -15.825 38.213 1.00 33.78 ? 64 LEU A CG 1 ATOM 511 C CD1 . LEU A 1 65 ? 37.429 -16.016 38.713 1.00 29.88 ? 64 LEU A CD1 1 ATOM 512 C CD2 . LEU A 1 65 ? 34.950 -16.349 39.230 1.00 27.43 ? 64 LEU A CD2 1 ATOM 513 N N . PHE A 1 66 ? 33.920 -11.610 37.979 1.00 33.33 ? 65 PHE A N 1 ATOM 514 C CA . PHE A 1 66 ? 34.136 -10.176 38.031 1.00 29.31 ? 65 PHE A CA 1 ATOM 515 C C . PHE A 1 66 ? 35.442 -9.915 38.762 1.00 40.41 ? 65 PHE A C 1 ATOM 516 O O . PHE A 1 66 ? 35.740 -10.541 39.781 1.00 42.08 ? 65 PHE A O 1 ATOM 517 C CB . PHE A 1 66 ? 32.970 -9.467 38.723 1.00 34.61 ? 65 PHE A CB 1 ATOM 518 C CG . PHE A 1 66 ? 31.902 -8.993 37.762 1.00 37.36 ? 65 PHE A CG 1 ATOM 519 C CD1 . PHE A 1 66 ? 32.127 -7.890 36.960 1.00 31.33 ? 65 PHE A CD1 1 ATOM 520 C CD2 . PHE A 1 66 ? 30.687 -9.676 37.639 1.00 32.92 ? 65 PHE A CD2 1 ATOM 521 C CE1 . PHE A 1 66 ? 31.171 -7.458 36.059 1.00 34.03 ? 65 PHE A CE1 1 ATOM 522 C CE2 . PHE A 1 66 ? 29.714 -9.249 36.744 1.00 31.66 ? 65 PHE A CE2 1 ATOM 523 C CZ . PHE A 1 66 ? 29.954 -8.145 35.946 1.00 31.82 ? 65 PHE A CZ 1 ATOM 524 N N . LYS A 1 67 ? 36.244 -9.008 38.219 1.00 46.10 ? 66 LYS A N 1 ATOM 525 C CA . LYS A 1 67 ? 37.511 -8.715 38.864 1.00 47.90 ? 66 LYS A CA 1 ATOM 526 C C . LYS A 1 67 ? 37.301 -8.099 40.250 1.00 52.58 ? 66 LYS A C 1 ATOM 527 O O . LYS A 1 67 ? 37.992 -8.473 41.205 1.00 49.13 ? 66 LYS A O 1 ATOM 528 C CB . LYS A 1 67 ? 38.360 -7.815 37.969 1.00 44.97 ? 66 LYS A CB 1 ATOM 529 C CG . LYS A 1 67 ? 39.722 -7.506 38.542 1.00 45.54 ? 66 LYS A CG 1 ATOM 530 C CD . LYS A 1 67 ? 40.418 -6.425 37.733 1.00 53.03 ? 66 LYS A CD 1 ATOM 531 C CE . LYS A 1 67 ? 41.717 -5.994 38.383 1.00 51.02 ? 66 LYS A CE 1 ATOM 532 N NZ . LYS A 1 67 ? 42.678 -7.110 38.408 1.00 54.21 ? 66 LYS A NZ 1 ATOM 533 N N . ASN A 1 68 ? 36.337 -7.188 40.406 1.00 51.59 ? 67 ASN A N 1 ATOM 534 C CA . ASN A 1 68 ? 36.184 -6.559 41.716 1.00 56.83 ? 67 ASN A CA 1 ATOM 535 C C . ASN A 1 68 ? 34.744 -6.103 41.944 1.00 50.16 ? 67 ASN A C 1 ATOM 536 O O . ASN A 1 68 ? 33.868 -6.263 41.089 1.00 49.84 ? 67 ASN A O 1 ATOM 537 C CB . ASN A 1 68 ? 37.188 -5.407 41.878 1.00 52.78 ? 67 ASN A CB 1 ATOM 538 C CG . ASN A 1 68 ? 37.164 -4.442 40.719 1.00 51.94 ? 67 ASN A CG 1 ATOM 539 O OD1 . ASN A 1 68 ? 36.102 -4.075 40.241 1.00 54.81 ? 67 ASN A OD1 1 ATOM 540 N ND2 . ASN A 1 68 ? 38.340 -4.024 40.260 1.00 53.98 ? 67 ASN A ND2 1 ATOM 541 N N . TYR A 1 69 ? 34.505 -5.545 43.129 1.00 47.84 ? 68 TYR A N 1 ATOM 542 C CA . TYR A 1 69 ? 33.205 -5.004 43.513 1.00 52.86 ? 68 TYR A CA 1 ATOM 543 C C . TYR A 1 69 ? 32.997 -3.540 43.106 1.00 53.28 ? 68 TYR A C 1 ATOM 544 O O . TYR A 1 69 ? 31.902 -2.998 43.319 1.00 44.53 ? 68 TYR A O 1 ATOM 545 C CB . TYR A 1 69 ? 33.009 -5.147 45.028 1.00 53.31 ? 68 TYR A CB 1 ATOM 546 C CG . TYR A 1 69 ? 32.718 -6.563 45.474 1.00 56.95 ? 68 TYR A CG 1 ATOM 547 C CD1 . TYR A 1 69 ? 31.412 -7.042 45.507 1.00 55.81 ? 68 TYR A CD1 1 ATOM 548 C CD2 . TYR A 1 69 ? 33.749 -7.423 45.856 1.00 58.43 ? 68 TYR A CD2 1 ATOM 549 C CE1 . TYR A 1 69 ? 31.129 -8.341 45.908 1.00 64.67 ? 68 TYR A CE1 1 ATOM 550 C CE2 . TYR A 1 69 ? 33.479 -8.733 46.266 1.00 64.31 ? 68 TYR A CE2 1 ATOM 551 C CZ . TYR A 1 69 ? 32.162 -9.183 46.285 1.00 64.59 ? 68 TYR A CZ 1 ATOM 552 O OH . TYR A 1 69 ? 31.865 -10.467 46.686 1.00 56.57 ? 68 TYR A OH 1 ATOM 553 N N . SER A 1 70 ? 34.005 -2.886 42.532 1.00 46.65 ? 69 SER A N 1 ATOM 554 C CA . SER A 1 70 ? 33.859 -1.491 42.149 1.00 42.89 ? 69 SER A CA 1 ATOM 555 C C . SER A 1 70 ? 32.967 -1.356 40.925 1.00 45.89 ? 69 SER A C 1 ATOM 556 O O . SER A 1 70 ? 33.233 -1.972 39.890 1.00 48.78 ? 69 SER A O 1 ATOM 557 C CB . SER A 1 70 ? 35.223 -0.878 41.860 1.00 41.41 ? 69 SER A CB 1 ATOM 558 O OG . SER A 1 70 ? 35.047 0.343 41.166 1.00 40.64 ? 69 SER A OG 1 ATOM 559 N N . LEU A 1 71 ? 31.930 -0.508 41.031 1.00 46.25 ? 70 LEU A N 1 ATOM 560 C CA . LEU A 1 71 ? 31.032 -0.252 39.904 1.00 44.29 ? 70 LEU A CA 1 ATOM 561 C C . LEU A 1 71 ? 31.734 0.389 38.713 1.00 44.82 ? 70 LEU A C 1 ATOM 562 O O . LEU A 1 71 ? 31.194 0.340 37.605 1.00 51.20 ? 70 LEU A O 1 ATOM 563 C CB . LEU A 1 71 ? 29.854 0.636 40.321 1.00 41.45 ? 70 LEU A CB 1 ATOM 564 C CG . LEU A 1 71 ? 28.578 -0.057 40.814 1.00 38.92 ? 70 LEU A CG 1 ATOM 565 C CD1 . LEU A 1 71 ? 27.994 -1.001 39.774 1.00 33.33 ? 70 LEU A CD1 1 ATOM 566 C CD2 . LEU A 1 71 ? 28.862 -0.819 42.092 1.00 44.29 ? 70 LEU A CD2 1 ATOM 567 N N . ASN A 1 72 ? 32.910 0.980 38.905 1.00 42.33 ? 71 ASN A N 1 ATOM 568 C CA . ASN A 1 72 ? 33.676 1.599 37.828 1.00 51.97 ? 71 ASN A CA 1 ATOM 569 C C . ASN A 1 72 ? 34.651 0.639 37.151 1.00 47.90 ? 71 ASN A C 1 ATOM 570 O O . ASN A 1 72 ? 35.352 1.034 36.211 1.00 40.38 ? 71 ASN A O 1 ATOM 571 C CB . ASN A 1 72 ? 34.427 2.816 38.374 1.00 53.26 ? 71 ASN A CB 1 ATOM 572 C CG . ASN A 1 72 ? 33.506 3.987 38.613 1.00 54.34 ? 71 ASN A CG 1 ATOM 573 O OD1 . ASN A 1 72 ? 32.758 4.024 39.587 1.00 57.07 ? 71 ASN A OD1 1 ATOM 574 N ND2 . ASN A 1 72 ? 33.529 4.938 37.703 1.00 63.70 ? 71 ASN A ND2 1 ATOM 575 N N . ASP A 1 73 ? 34.698 -0.606 37.598 1.00 45.31 ? 72 ASP A N 1 ATOM 576 C CA . ASP A 1 73 ? 35.533 -1.641 37.000 1.00 50.70 ? 72 ASP A CA 1 ATOM 577 C C . ASP A 1 73 ? 34.620 -2.785 36.557 1.00 43.51 ? 72 ASP A C 1 ATOM 578 O O . ASP A 1 73 ? 34.163 -3.579 37.382 1.00 47.48 ? 72 ASP A O 1 ATOM 579 C CB . ASP A 1 73 ? 36.577 -2.113 37.998 1.00 51.25 ? 72 ASP A CB 1 ATOM 580 C CG . ASP A 1 73 ? 37.744 -2.772 37.340 1.00 50.82 ? 72 ASP A CG 1 ATOM 581 O OD1 . ASP A 1 73 ? 37.608 -3.134 36.148 1.00 43.55 ? 72 ASP A OD1 1 ATOM 582 O OD2 . ASP A 1 73 ? 38.785 -2.938 38.025 1.00 50.60 ? 72 ASP A OD2 1 ATOM 583 N N . ALA A 1 74 ? 34.326 -2.858 35.263 1.00 36.93 ? 73 ALA A N 1 ATOM 584 C CA . ALA A 1 74 ? 33.475 -3.912 34.724 1.00 39.64 ? 73 ALA A CA 1 ATOM 585 C C . ALA A 1 74 ? 34.285 -5.085 34.205 1.00 39.18 ? 73 ALA A C 1 ATOM 586 O O . ALA A 1 74 ? 33.722 -5.997 33.600 1.00 41.85 ? 73 ALA A O 1 ATOM 587 C CB . ALA A 1 74 ? 32.580 -3.367 33.608 1.00 36.42 ? 73 ALA A CB 1 ATOM 588 N N . THR A 1 75 ? 35.590 -5.080 34.447 1.00 39.58 ? 74 THR A N 1 ATOM 589 C CA . THR A 1 75 ? 36.470 -6.091 33.900 1.00 31.62 ? 74 THR A CA 1 ATOM 590 C C . THR A 1 75 ? 36.091 -7.462 34.418 1.00 29.73 ? 74 THR A C 1 ATOM 591 O O . THR A 1 75 ? 35.848 -7.644 35.615 1.00 32.74 ? 74 THR A O 1 ATOM 592 C CB . THR A 1 75 ? 37.919 -5.757 34.259 1.00 39.51 ? 74 THR A CB 1 ATOM 593 O OG1 . THR A 1 75 ? 38.276 -4.519 33.629 1.00 44.91 ? 74 THR A OG1 1 ATOM 594 C CG2 . THR A 1 75 ? 38.866 -6.840 33.772 1.00 31.70 ? 74 THR A CG2 1 ATOM 595 N N . ILE A 1 76 ? 36.020 -8.422 33.495 1.00 30.57 ? 75 ILE A N 1 ATOM 596 C CA . ILE A 1 76 ? 35.754 -9.817 33.802 1.00 27.30 ? 75 ILE A CA 1 ATOM 597 C C . ILE A 1 76 ? 36.878 -10.676 33.242 1.00 29.51 ? 75 ILE A C 1 ATOM 598 O O . ILE A 1 76 ? 37.644 -10.263 32.363 1.00 30.04 ? 75 ILE A O 1 ATOM 599 C CB . ILE A 1 76 ? 34.409 -10.289 33.227 1.00 25.71 ? 75 ILE A CB 1 ATOM 600 C CG1 . ILE A 1 76 ? 34.461 -10.249 31.696 1.00 24.45 ? 75 ILE A CG1 1 ATOM 601 C CG2 . ILE A 1 76 ? 33.278 -9.428 33.751 1.00 25.94 ? 75 ILE A CG2 1 ATOM 602 C CD1 . ILE A 1 76 ? 33.166 -10.714 31.006 1.00 26.84 ? 75 ILE A CD1 1 ATOM 603 N N . THR A 1 77 ? 36.962 -11.890 33.763 1.00 29.98 ? 76 THR A N 1 ATOM 604 C CA . THR A 1 77 ? 37.789 -12.927 33.174 1.00 28.28 ? 76 THR A CA 1 ATOM 605 C C . THR A 1 77 ? 36.904 -14.099 32.773 1.00 29.69 ? 76 THR A C 1 ATOM 606 O O . THR A 1 77 ? 35.966 -14.472 33.487 1.00 27.44 ? 76 THR A O 1 ATOM 607 C CB . THR A 1 77 ? 38.926 -13.394 34.116 1.00 32.11 ? 76 THR A CB 1 ATOM 608 O OG1 . THR A 1 77 ? 38.407 -13.825 35.389 1.00 37.01 ? 76 THR A OG1 1 ATOM 609 C CG2 . THR A 1 77 ? 39.885 -12.279 34.337 1.00 29.41 ? 76 THR A CG2 1 ATOM 610 N N . LEU A 1 78 ? 37.229 -14.656 31.615 1.00 37.31 ? 77 LEU A N 1 ATOM 611 C CA . LEU A 1 78 ? 36.497 -15.719 30.956 1.00 27.28 ? 77 LEU A CA 1 ATOM 612 C C . LEU A 1 78 ? 37.416 -16.923 30.886 1.00 24.87 ? 77 LEU A C 1 ATOM 613 O O . LEU A 1 78 ? 38.590 -16.782 30.546 1.00 27.74 ? 77 LEU A O 1 ATOM 614 C CB . LEU A 1 78 ? 36.074 -15.268 29.560 1.00 27.09 ? 77 LEU A CB 1 ATOM 615 C CG . LEU A 1 78 ? 35.277 -16.276 28.753 1.00 33.20 ? 77 LEU A CG 1 ATOM 616 C CD1 . LEU A 1 78 ? 34.006 -16.659 29.483 1.00 26.01 ? 77 LEU A CD1 1 ATOM 617 C CD2 . LEU A 1 78 ? 34.971 -15.644 27.427 1.00 34.89 ? 77 LEU A CD2 1 ATOM 618 N N . HIS A 1 79 ? 36.884 -18.092 31.229 1.00 31.38 ? 78 HIS A N 1 ATOM 619 C CA . HIS A 1 79 ? 37.668 -19.293 31.487 1.00 28.50 ? 78 HIS A CA 1 ATOM 620 C C . HIS A 1 79 ? 37.057 -20.455 30.723 1.00 27.85 ? 78 HIS A C 1 ATOM 621 O O . HIS A 1 79 ? 35.890 -20.406 30.321 1.00 25.81 ? 78 HIS A O 1 ATOM 622 C CB . HIS A 1 79 ? 37.707 -19.625 32.991 1.00 30.79 ? 78 HIS A CB 1 ATOM 623 C CG . HIS A 1 79 ? 38.276 -18.534 33.839 1.00 28.13 ? 78 HIS A CG 1 ATOM 624 N ND1 . HIS A 1 79 ? 39.502 -18.640 34.463 1.00 34.55 ? 78 HIS A ND1 1 ATOM 625 C CD2 . HIS A 1 79 ? 37.798 -17.307 34.159 1.00 30.70 ? 78 HIS A CD2 1 ATOM 626 C CE1 . HIS A 1 79 ? 39.756 -17.527 35.133 1.00 25.99 ? 78 HIS A CE1 1 ATOM 627 N NE2 . HIS A 1 79 ? 38.741 -16.699 34.961 1.00 30.14 ? 78 HIS A NE2 1 ATOM 628 N N . ASN A 1 80 ? 37.846 -21.512 30.546 1.00 26.51 ? 79 ASN A N 1 ATOM 629 C CA . ASN A 1 80 ? 37.485 -22.631 29.668 1.00 30.69 ? 79 ASN A CA 1 ATOM 630 C C . ASN A 1 80 ? 36.944 -22.114 28.340 1.00 32.14 ? 79 ASN A C 1 ATOM 631 O O . ASN A 1 80 ? 35.790 -22.342 27.972 1.00 32.63 ? 79 ASN A O 1 ATOM 632 C CB . ASN A 1 80 ? 36.468 -23.569 30.323 1.00 29.38 ? 79 ASN A CB 1 ATOM 633 C CG . ASN A 1 80 ? 37.082 -24.418 31.405 1.00 37.43 ? 79 ASN A CG 1 ATOM 634 O OD1 . ASN A 1 80 ? 36.649 -24.381 32.557 1.00 38.86 ? 79 ASN A OD1 1 ATOM 635 N ND2 . ASN A 1 80 ? 38.114 -25.181 31.048 1.00 29.54 ? 79 ASN A ND2 1 ATOM 636 N N . ILE A 1 81 ? 37.807 -21.394 27.630 1.00 29.34 ? 80 ILE A N 1 ATOM 637 C CA . ILE A 1 81 ? 37.372 -20.665 26.454 1.00 26.50 ? 80 ILE A CA 1 ATOM 638 C C . ILE A 1 81 ? 36.954 -21.645 25.373 1.00 32.79 ? 80 ILE A C 1 ATOM 639 O O . ILE A 1 81 ? 37.599 -22.688 25.168 1.00 28.63 ? 80 ILE A O 1 ATOM 640 C CB . ILE A 1 81 ? 38.483 -19.710 25.996 1.00 28.78 ? 80 ILE A CB 1 ATOM 641 C CG1 . ILE A 1 81 ? 38.432 -18.463 26.888 1.00 30.69 ? 80 ILE A CG1 1 ATOM 642 C CG2 . ILE A 1 81 ? 38.320 -19.356 24.538 1.00 26.62 ? 80 ILE A CG2 1 ATOM 643 C CD1 . ILE A 1 81 ? 39.624 -17.569 26.802 1.00 37.48 ? 80 ILE A CD1 1 ATOM 644 N N . GLY A 1 82 ? 35.828 -21.334 24.713 1.00 28.31 ? 81 GLY A N 1 ATOM 645 C CA . GLY A 1 82 ? 35.208 -22.220 23.754 1.00 21.59 ? 81 GLY A CA 1 ATOM 646 C C . GLY A 1 82 ? 35.024 -21.486 22.437 1.00 24.29 ? 81 GLY A C 1 ATOM 647 O O . GLY A 1 82 ? 35.142 -20.258 22.374 1.00 33.75 ? 81 GLY A O 1 ATOM 648 N N . PHE A 1 83 ? 34.730 -22.251 21.380 1.00 23.25 ? 82 PHE A N 1 ATOM 649 C CA . PHE A 1 83 ? 34.513 -21.637 20.070 1.00 21.06 ? 82 PHE A CA 1 ATOM 650 C C . PHE A 1 83 ? 33.433 -20.577 20.118 1.00 22.23 ? 82 PHE A C 1 ATOM 651 O O . PHE A 1 83 ? 33.576 -19.510 19.509 1.00 27.59 ? 82 PHE A O 1 ATOM 652 C CB . PHE A 1 83 ? 34.164 -22.688 19.026 1.00 21.53 ? 82 PHE A CB 1 ATOM 653 C CG . PHE A 1 83 ? 35.336 -23.523 18.596 1.00 27.61 ? 82 PHE A CG 1 ATOM 654 C CD1 . PHE A 1 83 ? 36.414 -22.942 17.930 1.00 28.06 ? 82 PHE A CD1 1 ATOM 655 C CD2 . PHE A 1 83 ? 35.367 -24.889 18.846 1.00 27.15 ? 82 PHE A CD2 1 ATOM 656 C CE1 . PHE A 1 83 ? 37.501 -23.712 17.519 1.00 24.07 ? 82 PHE A CE1 1 ATOM 657 C CE2 . PHE A 1 83 ? 36.468 -25.671 18.455 1.00 24.87 ? 82 PHE A CE2 1 ATOM 658 C CZ . PHE A 1 83 ? 37.527 -25.080 17.781 1.00 26.77 ? 82 PHE A CZ 1 ATOM 659 N N . SER A 1 84 ? 32.353 -20.829 20.851 1.00 28.45 ? 83 SER A N 1 ATOM 660 C CA . SER A 1 84 ? 31.251 -19.871 20.819 1.00 26.22 ? 83 SER A CA 1 ATOM 661 C C . SER A 1 84 ? 31.596 -18.565 21.529 1.00 32.93 ? 83 SER A C 1 ATOM 662 O O . SER A 1 84 ? 30.880 -17.569 21.347 1.00 27.70 ? 83 SER A O 1 ATOM 663 C CB . SER A 1 84 ? 29.990 -20.512 21.404 1.00 21.28 ? 83 SER A CB 1 ATOM 664 O OG . SER A 1 84 ? 30.177 -20.915 22.750 1.00 33.48 ? 83 SER A OG 1 ATOM 665 N N . ASP A 1 85 ? 32.697 -18.527 22.290 1.00 28.42 ? 84 ASP A N 1 ATOM 666 C CA . ASP A 1 85 ? 33.079 -17.272 22.924 1.00 33.20 ? 84 ASP A CA 1 ATOM 667 C C . ASP A 1 85 ? 33.614 -16.261 21.927 1.00 27.50 ? 84 ASP A C 1 ATOM 668 O O . ASP A 1 85 ? 33.787 -15.095 22.285 1.00 31.55 ? 84 ASP A O 1 ATOM 669 C CB . ASP A 1 85 ? 34.109 -17.527 24.018 1.00 25.80 ? 84 ASP A CB 1 ATOM 670 C CG . ASP A 1 85 ? 33.542 -18.335 25.163 1.00 27.09 ? 84 ASP A CG 1 ATOM 671 O OD1 . ASP A 1 85 ? 32.335 -18.204 25.448 1.00 31.42 ? 84 ASP A OD1 1 ATOM 672 O OD2 . ASP A 1 85 ? 34.289 -19.123 25.764 1.00 28.87 ? 84 ASP A OD2 1 ATOM 673 N N . SER A 1 86 ? 33.870 -16.682 20.699 1.00 25.54 ? 85 SER A N 1 ATOM 674 C CA . SER A 1 86 ? 34.269 -15.777 19.634 1.00 31.38 ? 85 SER A CA 1 ATOM 675 C C . SER A 1 86 ? 33.133 -14.817 19.279 1.00 30.56 ? 85 SER A C 1 ATOM 676 O O . SER A 1 86 ? 31.957 -15.156 19.371 1.00 34.42 ? 85 SER A O 1 ATOM 677 C CB . SER A 1 86 ? 34.685 -16.594 18.409 1.00 30.61 ? 85 SER A CB 1 ATOM 678 O OG . SER A 1 86 ? 34.938 -15.770 17.292 1.00 44.40 ? 85 SER A OG 1 ATOM 679 N N . GLY A 1 87 ? 33.488 -13.605 18.893 1.00 29.02 ? 86 GLY A N 1 ATOM 680 C CA . GLY A 1 87 ? 32.490 -12.665 18.440 1.00 30.60 ? 86 GLY A CA 1 ATOM 681 C C . GLY A 1 87 ? 32.722 -11.286 19.024 1.00 34.08 ? 86 GLY A C 1 ATOM 682 O O . GLY A 1 87 ? 33.805 -10.970 19.513 1.00 28.42 ? 86 GLY A O 1 ATOM 683 N N . LYS A 1 88 ? 31.675 -10.463 18.975 1.00 37.54 ? 87 LYS A N 1 ATOM 684 C CA . LYS A 1 88 ? 31.770 -9.072 19.390 1.00 34.55 ? 87 LYS A CA 1 ATOM 685 C C . LYS A 1 88 ? 30.996 -8.869 20.679 1.00 31.36 ? 87 LYS A C 1 ATOM 686 O O . LYS A 1 88 ? 29.841 -9.287 20.792 1.00 36.57 ? 87 LYS A O 1 ATOM 687 C CB . LYS A 1 88 ? 31.252 -8.120 18.308 1.00 38.27 ? 87 LYS A CB 1 ATOM 688 C CG . LYS A 1 88 ? 31.793 -6.697 18.505 1.00 50.96 ? 87 LYS A CG 1 ATOM 689 C CD . LYS A 1 88 ? 30.908 -5.621 17.931 1.00 51.82 ? 87 LYS A CD 1 ATOM 690 C CE . LYS A 1 88 ? 31.545 -4.919 16.737 1.00 61.95 ? 87 LYS A CE 1 ATOM 691 N NZ . LYS A 1 88 ? 30.565 -4.011 16.042 1.00 67.94 ? 87 LYS A NZ 1 ATOM 692 N N . TYR A 1 89 ? 31.636 -8.224 21.634 1.00 32.80 ? 88 TYR A N 1 ATOM 693 C CA . TYR A 1 89 ? 31.065 -7.895 22.926 1.00 30.72 ? 88 TYR A CA 1 ATOM 694 C C . TYR A 1 89 ? 30.970 -6.384 23.056 1.00 34.46 ? 88 TYR A C 1 ATOM 695 O O . TYR A 1 89 ? 31.674 -5.634 22.377 1.00 36.36 ? 88 TYR A O 1 ATOM 696 C CB . TYR A 1 89 ? 31.934 -8.439 24.064 1.00 30.76 ? 88 TYR A CB 1 ATOM 697 C CG . TYR A 1 89 ? 32.042 -9.944 24.154 1.00 30.66 ? 88 TYR A CG 1 ATOM 698 C CD1 . TYR A 1 89 ? 32.825 -10.661 23.261 1.00 25.56 ? 88 TYR A CD1 1 ATOM 699 C CD2 . TYR A 1 89 ? 31.413 -10.637 25.185 1.00 31.49 ? 88 TYR A CD2 1 ATOM 700 C CE1 . TYR A 1 89 ? 32.947 -12.023 23.365 1.00 33.88 ? 88 TYR A CE1 1 ATOM 701 C CE2 . TYR A 1 89 ? 31.536 -12.013 25.300 1.00 35.35 ? 88 TYR A CE2 1 ATOM 702 C CZ . TYR A 1 89 ? 32.303 -12.697 24.391 1.00 34.07 ? 88 TYR A CZ 1 ATOM 703 O OH . TYR A 1 89 ? 32.410 -14.054 24.504 1.00 27.07 ? 88 TYR A OH 1 ATOM 704 N N . ILE A 1 90 ? 30.106 -5.935 23.952 1.00 28.73 ? 89 ILE A N 1 ATOM 705 C CA . ILE A 1 90 ? 30.028 -4.522 24.280 1.00 32.05 ? 89 ILE A CA 1 ATOM 706 C C . ILE A 1 90 ? 30.038 -4.391 25.794 1.00 33.57 ? 89 ILE A C 1 ATOM 707 O O . ILE A 1 90 ? 29.265 -5.059 26.488 1.00 30.89 ? 89 ILE A O 1 ATOM 708 C CB . ILE A 1 90 ? 28.788 -3.832 23.660 1.00 31.15 ? 89 ILE A CB 1 ATOM 709 C CG1 . ILE A 1 90 ? 27.503 -4.527 24.036 1.00 37.60 ? 89 ILE A CG1 1 ATOM 710 C CG2 . ILE A 1 90 ? 28.861 -3.808 22.145 1.00 32.12 ? 89 ILE A CG2 1 ATOM 711 C CD1 . ILE A 1 90 ? 26.347 -3.594 24.053 1.00 47.39 ? 89 ILE A CD1 1 ATOM 712 N N . CYS A 1 91 ? 30.946 -3.569 26.310 1.00 34.49 ? 90 CYS A N 1 ATOM 713 C CA . CYS A 1 91 ? 30.839 -3.129 27.687 1.00 33.36 ? 90 CYS A CA 1 ATOM 714 C C . CYS A 1 91 ? 29.808 -2.011 27.733 1.00 35.28 ? 90 CYS A C 1 ATOM 715 O O . CYS A 1 91 ? 29.779 -1.158 26.846 1.00 46.96 ? 90 CYS A O 1 ATOM 716 C CB . CYS A 1 91 ? 32.203 -2.656 28.202 1.00 29.37 ? 90 CYS A CB 1 ATOM 717 S SG . CYS A 1 91 ? 32.163 -2.432 29.961 1.00 41.08 ? 90 CYS A SG 1 ATOM 718 N N . LYS A 1 92 ? 28.939 -2.022 28.741 1.00 35.51 ? 91 LYS A N 1 ATOM 719 C CA . LYS A 1 92 ? 27.826 -1.075 28.788 1.00 31.49 ? 91 LYS A CA 1 ATOM 720 C C . LYS A 1 92 ? 27.593 -0.585 30.217 1.00 31.35 ? 91 LYS A C 1 ATOM 721 O O . LYS A 1 92 ? 27.350 -1.382 31.126 1.00 36.44 ? 91 LYS A O 1 ATOM 722 C CB . LYS A 1 92 ? 26.556 -1.713 28.209 1.00 32.93 ? 91 LYS A CB 1 ATOM 723 C CG . LYS A 1 92 ? 25.405 -0.771 28.109 1.00 37.50 ? 91 LYS A CG 1 ATOM 724 C CD . LYS A 1 92 ? 24.093 -1.466 27.862 1.00 44.14 ? 91 LYS A CD 1 ATOM 725 C CE . LYS A 1 92 ? 24.023 -2.070 26.480 1.00 55.29 ? 91 LYS A CE 1 ATOM 726 N NZ . LYS A 1 92 ? 22.654 -2.623 26.203 1.00 68.85 ? 91 LYS A NZ 1 ATOM 727 N N . ALA A 1 93 ? 27.674 0.726 30.419 1.00 37.57 ? 92 ALA A N 1 ATOM 728 C CA . ALA A 1 93 ? 27.326 1.366 31.684 1.00 35.73 ? 92 ALA A CA 1 ATOM 729 C C . ALA A 1 93 ? 26.015 2.131 31.521 1.00 42.43 ? 92 ALA A C 1 ATOM 730 O O . ALA A 1 93 ? 25.925 3.039 30.692 1.00 46.42 ? 92 ALA A O 1 ATOM 731 C CB . ALA A 1 93 ? 28.424 2.320 32.134 1.00 29.64 ? 92 ALA A CB 1 ATOM 732 N N . VAL A 1 94 ? 25.006 1.758 32.295 1.00 30.96 ? 93 VAL A N 1 ATOM 733 C CA . VAL A 1 94 ? 23.769 2.513 32.375 1.00 32.34 ? 93 VAL A CA 1 ATOM 734 C C . VAL A 1 94 ? 23.925 3.485 33.529 1.00 37.90 ? 93 VAL A C 1 ATOM 735 O O . VAL A 1 94 ? 24.292 3.084 34.638 1.00 35.61 ? 93 VAL A O 1 ATOM 736 C CB . VAL A 1 94 ? 22.557 1.583 32.584 1.00 37.36 ? 93 VAL A CB 1 ATOM 737 C CG1 . VAL A 1 94 ? 21.250 2.382 32.684 1.00 34.58 ? 93 VAL A CG1 1 ATOM 738 C CG2 . VAL A 1 94 ? 22.449 0.542 31.452 1.00 36.08 ? 93 VAL A CG2 1 ATOM 739 N N . THR A 1 95 ? 23.680 4.768 33.271 1.00 41.69 ? 94 THR A N 1 ATOM 740 C CA . THR A 1 95 ? 23.874 5.800 34.282 1.00 44.05 ? 94 THR A CA 1 ATOM 741 C C . THR A 1 95 ? 22.565 6.531 34.582 1.00 35.58 ? 94 THR A C 1 ATOM 742 O O . THR A 1 95 ? 21.587 6.447 33.837 1.00 31.31 ? 94 THR A O 1 ATOM 743 C CB . THR A 1 95 ? 24.977 6.800 33.858 1.00 44.99 ? 94 THR A CB 1 ATOM 744 O OG1 . THR A 1 95 ? 24.644 7.413 32.608 1.00 41.21 ? 94 THR A OG1 1 ATOM 745 C CG2 . THR A 1 95 ? 26.317 6.093 33.701 1.00 40.30 ? 94 THR A CG2 1 ATOM 746 N N . PHE A 1 96 ? 22.550 7.206 35.723 1.00 32.90 ? 95 PHE A N 1 ATOM 747 C CA . PHE A 1 96 ? 21.450 8.063 36.106 1.00 32.50 ? 95 PHE A CA 1 ATOM 748 C C . PHE A 1 96 ? 21.883 9.539 36.193 1.00 41.59 ? 95 PHE A C 1 ATOM 749 O O . PHE A 1 96 ? 22.766 9.876 36.970 1.00 42.14 ? 95 PHE A O 1 ATOM 750 C CB . PHE A 1 96 ? 20.872 7.621 37.442 1.00 32.55 ? 95 PHE A CB 1 ATOM 751 C CG . PHE A 1 96 ? 19.669 8.438 37.875 1.00 39.46 ? 95 PHE A CG 1 ATOM 752 C CD1 . PHE A 1 96 ? 18.396 8.112 37.419 1.00 27.17 ? 95 PHE A CD1 1 ATOM 753 C CD2 . PHE A 1 96 ? 19.818 9.541 38.720 1.00 34.80 ? 95 PHE A CD2 1 ATOM 754 C CE1 . PHE A 1 96 ? 17.281 8.862 37.804 1.00 28.46 ? 95 PHE A CE1 1 ATOM 755 C CE2 . PHE A 1 96 ? 18.712 10.299 39.106 1.00 27.05 ? 95 PHE A CE2 1 ATOM 756 C CZ . PHE A 1 96 ? 17.443 9.961 38.651 1.00 28.33 ? 95 PHE A CZ 1 ATOM 757 N N . PRO A 1 97 ? 21.217 10.439 35.443 1.00 44.88 ? 96 PRO A N 1 ATOM 758 C CA . PRO A 1 97 ? 19.999 10.209 34.658 1.00 38.39 ? 96 PRO A CA 1 ATOM 759 C C . PRO A 1 97 ? 20.188 9.976 33.148 1.00 39.21 ? 96 PRO A C 1 ATOM 760 O O . PRO A 1 97 ? 19.251 9.537 32.471 1.00 44.39 ? 96 PRO A O 1 ATOM 761 C CB . PRO A 1 97 ? 19.221 11.510 34.886 1.00 36.33 ? 96 PRO A CB 1 ATOM 762 C CG . PRO A 1 97 ? 20.304 12.562 34.943 1.00 35.10 ? 96 PRO A CG 1 ATOM 763 C CD . PRO A 1 97 ? 21.535 11.880 35.527 1.00 41.65 ? 96 PRO A CD 1 ATOM 764 N N . LEU A 1 98 ? 21.371 10.246 32.609 1.00 27.62 ? 97 LEU A N 1 ATOM 765 C CA . LEU A 1 98 ? 21.447 10.303 31.160 1.00 35.09 ? 97 LEU A CA 1 ATOM 766 C C . LEU A 1 98 ? 21.382 8.943 30.467 1.00 45.55 ? 97 LEU A C 1 ATOM 767 O O . LEU A 1 98 ? 21.213 8.909 29.241 1.00 51.60 ? 97 LEU A O 1 ATOM 768 C CB . LEU A 1 98 ? 22.714 11.050 30.759 1.00 46.17 ? 97 LEU A CB 1 ATOM 769 C CG . LEU A 1 98 ? 22.771 12.492 31.274 1.00 50.37 ? 97 LEU A CG 1 ATOM 770 C CD1 . LEU A 1 98 ? 24.036 13.162 30.792 1.00 48.99 ? 97 LEU A CD1 1 ATOM 771 C CD2 . LEU A 1 98 ? 21.495 13.271 30.904 1.00 41.65 ? 97 LEU A CD2 1 ATOM 772 N N . GLY A 1 99 ? 21.505 7.832 31.191 1.00 42.23 ? 98 GLY A N 1 ATOM 773 C CA . GLY A 1 99 ? 21.350 6.525 30.574 1.00 42.59 ? 98 GLY A CA 1 ATOM 774 C C . GLY A 1 99 ? 22.644 5.835 30.181 1.00 49.88 ? 98 GLY A C 1 ATOM 775 O O . GLY A 1 99 ? 23.694 6.058 30.793 1.00 51.68 ? 98 GLY A O 1 ATOM 776 N N . ASN A 1 100 ? 22.583 5.011 29.138 1.00 47.66 ? 99 ASN A N 1 ATOM 777 C CA . ASN A 1 100 ? 23.649 4.067 28.833 1.00 51.47 ? 99 ASN A CA 1 ATOM 778 C C . ASN A 1 100 ? 24.749 4.674 27.960 1.00 59.60 ? 99 ASN A C 1 ATOM 779 O O . ASN A 1 100 ? 24.524 5.605 27.178 1.00 57.38 ? 99 ASN A O 1 ATOM 780 C CB . ASN A 1 100 ? 23.080 2.825 28.143 1.00 48.63 ? 99 ASN A CB 1 ATOM 781 C CG . ASN A 1 100 ? 22.546 3.133 26.777 1.00 59.19 ? 99 ASN A CG 1 ATOM 782 O OD1 . ASN A 1 100 ? 22.067 4.243 26.534 1.00 71.79 ? 99 ASN A OD1 1 ATOM 783 N ND2 . ASN A 1 100 ? 22.621 2.165 25.868 1.00 55.53 ? 99 ASN A ND2 1 ATOM 784 N N . ALA A 1 101 ? 25.954 4.127 28.124 1.00 52.69 ? 100 ALA A N 1 ATOM 785 C CA . ALA A 1 101 ? 27.102 4.379 27.270 1.00 50.02 ? 100 ALA A CA 1 ATOM 786 C C . ALA A 1 101 ? 27.798 3.045 27.069 1.00 49.07 ? 100 ALA A C 1 ATOM 787 O O . ALA A 1 101 ? 27.698 2.160 27.918 1.00 40.02 ? 100 ALA A O 1 ATOM 788 C CB . ALA A 1 101 ? 28.066 5.404 27.883 1.00 49.94 ? 100 ALA A CB 1 ATOM 789 N N . GLN A 1 102 ? 28.497 2.893 25.944 1.00 54.94 ? 101 GLN A N 1 ATOM 790 C CA . GLN A 1 102 ? 29.018 1.579 25.604 1.00 47.50 ? 101 GLN A CA 1 ATOM 791 C C . GLN A 1 102 ? 30.240 1.681 24.704 1.00 49.64 ? 101 GLN A C 1 ATOM 792 O O . GLN A 1 102 ? 30.507 2.714 24.091 1.00 52.14 ? 101 GLN A O 1 ATOM 793 C CB . GLN A 1 102 ? 27.945 0.723 24.927 1.00 43.95 ? 101 GLN A CB 1 ATOM 794 C CG . GLN A 1 102 ? 27.571 1.125 23.515 1.00 33.87 ? 101 GLN A CG 1 ATOM 795 C CD . GLN A 1 102 ? 26.504 0.204 22.932 1.00 45.15 ? 101 GLN A CD 1 ATOM 796 O OE1 . GLN A 1 102 ? 25.478 -0.062 23.569 1.00 54.72 ? 101 GLN A OE1 1 ATOM 797 N NE2 . GLN A 1 102 ? 26.745 -0.299 21.727 1.00 44.94 ? 101 GLN A NE2 1 ATOM 798 N N . SER A 1 103 ? 30.973 0.570 24.632 1.00 45.14 ? 102 SER A N 1 ATOM 799 C CA . SER A 1 103 ? 32.108 0.390 23.736 1.00 46.33 ? 102 SER A CA 1 ATOM 800 C C . SER A 1 103 ? 32.276 -1.103 23.494 1.00 48.42 ? 102 SER A C 1 ATOM 801 O O . SER A 1 103 ? 31.913 -1.928 24.342 1.00 45.40 ? 102 SER A O 1 ATOM 802 C CB . SER A 1 103 ? 33.408 0.974 24.312 1.00 53.44 ? 102 SER A CB 1 ATOM 803 O OG . SER A 1 103 ? 33.360 2.385 24.428 1.00 61.27 ? 102 SER A OG 1 ATOM 804 N N . SER A 1 104 ? 32.846 -1.449 22.345 1.00 42.00 ? 103 SER A N 1 ATOM 805 C CA . SER A 1 104 ? 32.892 -2.829 21.900 1.00 37.27 ? 103 SER A CA 1 ATOM 806 C C . SER A 1 104 ? 34.306 -3.393 21.996 1.00 43.58 ? 103 SER A C 1 ATOM 807 O O . SER A 1 104 ? 35.290 -2.664 21.890 1.00 44.37 ? 103 SER A O 1 ATOM 808 C CB . SER A 1 104 ? 32.385 -2.956 20.466 1.00 38.55 ? 103 SER A CB 1 ATOM 809 O OG . SER A 1 104 ? 33.270 -2.294 19.590 1.00 47.56 ? 103 SER A OG 1 ATOM 810 N N . THR A 1 105 ? 34.379 -4.708 22.221 1.00 39.01 ? 104 THR A N 1 ATOM 811 C CA . THR A 1 105 ? 35.594 -5.508 22.165 1.00 39.22 ? 104 THR A CA 1 ATOM 812 C C . THR A 1 105 ? 35.286 -6.731 21.318 1.00 41.20 ? 104 THR A C 1 ATOM 813 O O . THR A 1 105 ? 34.245 -7.366 21.512 1.00 39.05 ? 104 THR A O 1 ATOM 814 C CB . THR A 1 105 ? 36.044 -5.964 23.559 1.00 39.53 ? 104 THR A CB 1 ATOM 815 O OG1 . THR A 1 105 ? 36.550 -4.859 24.315 1.00 43.47 ? 104 THR A OG1 1 ATOM 816 C CG2 . THR A 1 105 ? 37.108 -7.019 23.443 1.00 42.03 ? 104 THR A CG2 1 ATOM 817 N N . THR A 1 106 ? 36.171 -7.062 20.385 1.00 40.97 ? 105 THR A N 1 ATOM 818 C CA . THR A 1 106 ? 35.992 -8.234 19.538 1.00 38.71 ? 105 THR A CA 1 ATOM 819 C C . THR A 1 106 ? 36.992 -9.312 19.944 1.00 40.04 ? 105 THR A C 1 ATOM 820 O O . THR A 1 106 ? 38.162 -9.020 20.212 1.00 38.53 ? 105 THR A O 1 ATOM 821 C CB . THR A 1 106 ? 36.149 -7.866 18.063 1.00 40.01 ? 105 THR A CB 1 ATOM 822 O OG1 . THR A 1 106 ? 35.133 -6.919 17.713 1.00 44.61 ? 105 THR A OG1 1 ATOM 823 C CG2 . THR A 1 106 ? 36.005 -9.073 17.184 1.00 30.16 ? 105 THR A CG2 1 ATOM 824 N N . VAL A 1 107 ? 36.517 -10.556 20.009 1.00 30.01 ? 106 VAL A N 1 ATOM 825 C CA . VAL A 1 107 ? 37.275 -11.671 20.561 1.00 31.27 ? 106 VAL A CA 1 ATOM 826 C C . VAL A 1 107 ? 37.476 -12.713 19.475 1.00 35.44 ? 106 VAL A C 1 ATOM 827 O O . VAL A 1 107 ? 36.509 -13.165 18.858 1.00 33.57 ? 106 VAL A O 1 ATOM 828 C CB . VAL A 1 107 ? 36.566 -12.279 21.784 1.00 31.99 ? 106 VAL A CB 1 ATOM 829 C CG1 . VAL A 1 107 ? 37.095 -13.679 22.092 1.00 31.02 ? 106 VAL A CG1 1 ATOM 830 C CG2 . VAL A 1 107 ? 36.760 -11.372 22.969 1.00 35.52 ? 106 VAL A CG2 1 ATOM 831 N N . THR A 1 108 ? 38.731 -13.082 19.241 1.00 37.37 ? 107 THR A N 1 ATOM 832 C CA . THR A 1 108 ? 39.084 -14.189 18.367 1.00 35.44 ? 107 THR A CA 1 ATOM 833 C C . THR A 1 108 ? 39.545 -15.371 19.213 1.00 32.51 ? 107 THR A C 1 ATOM 834 O O . THR A 1 108 ? 40.284 -15.190 20.183 1.00 30.16 ? 107 THR A O 1 ATOM 835 C CB . THR A 1 108 ? 40.197 -13.785 17.404 1.00 40.35 ? 107 THR A CB 1 ATOM 836 O OG1 . THR A 1 108 ? 39.785 -12.641 16.648 1.00 48.86 ? 107 THR A OG1 1 ATOM 837 C CG2 . THR A 1 108 ? 40.510 -14.932 16.457 1.00 34.55 ? 107 THR A CG2 1 ATOM 838 N N . VAL A 1 109 ? 39.100 -16.577 18.856 1.00 31.47 ? 108 VAL A N 1 ATOM 839 C CA . VAL A 1 109 ? 39.444 -17.791 19.585 1.00 21.61 ? 108 VAL A CA 1 ATOM 840 C C . VAL A 1 109 ? 40.417 -18.580 18.721 1.00 32.63 ? 108 VAL A C 1 ATOM 841 O O . VAL A 1 109 ? 40.112 -18.910 17.568 1.00 34.36 ? 108 VAL A O 1 ATOM 842 C CB . VAL A 1 109 ? 38.199 -18.627 19.937 1.00 28.09 ? 108 VAL A CB 1 ATOM 843 C CG1 . VAL A 1 109 ? 38.578 -19.946 20.587 1.00 26.37 ? 108 VAL A CG1 1 ATOM 844 C CG2 . VAL A 1 109 ? 37.301 -17.890 20.888 1.00 26.66 ? 108 VAL A CG2 1 ATOM 845 N N . LEU A 1 110 ? 41.600 -18.855 19.265 1.00 30.30 ? 109 LEU A N 1 ATOM 846 C CA . LEU A 1 110 ? 42.606 -19.665 18.603 1.00 25.05 ? 109 LEU A CA 1 ATOM 847 C C . LEU A 1 110 ? 42.693 -21.000 19.320 1.00 26.11 ? 109 LEU A C 1 ATOM 848 O O . LEU A 1 110 ? 42.355 -21.099 20.500 1.00 34.45 ? 109 LEU A O 1 ATOM 849 C CB . LEU A 1 110 ? 43.965 -18.967 18.623 1.00 32.71 ? 109 LEU A CB 1 ATOM 850 C CG . LEU A 1 110 ? 44.088 -17.521 18.109 1.00 28.70 ? 109 LEU A CG 1 ATOM 851 C CD1 . LEU A 1 110 ? 45.542 -17.163 18.129 1.00 31.10 ? 109 LEU A CD1 1 ATOM 852 C CD2 . LEU A 1 110 ? 43.543 -17.332 16.710 1.00 25.27 ? 109 LEU A CD2 1 ATOM 853 N N . VAL A 1 111 ? 43.132 -22.034 18.614 1.00 27.73 ? 110 VAL A N 1 ATOM 854 C CA . VAL A 1 111 ? 43.340 -23.348 19.214 1.00 26.20 ? 110 VAL A CA 1 ATOM 855 C C . VAL A 1 111 ? 44.800 -23.748 19.027 1.00 31.53 ? 110 VAL A C 1 ATOM 856 O O . VAL A 1 111 ? 45.310 -23.738 17.898 1.00 31.18 ? 110 VAL A O 1 ATOM 857 C CB . VAL A 1 111 ? 42.411 -24.409 18.602 1.00 28.70 ? 110 VAL A CB 1 ATOM 858 C CG1 . VAL A 1 111 ? 42.572 -25.755 19.352 1.00 26.34 ? 110 VAL A CG1 1 ATOM 859 C CG2 . VAL A 1 111 ? 40.977 -23.918 18.619 1.00 30.33 ? 110 VAL A CG2 1 ATOM 860 N N . GLU A 1 112 ? 45.464 -24.109 20.127 1.00 31.54 ? 111 GLU A N 1 ATOM 861 C CA . GLU A 1 112 ? 46.860 -24.532 20.036 1.00 35.07 ? 111 GLU A CA 1 ATOM 862 C C . GLU A 1 112 ? 46.952 -25.871 19.323 1.00 31.18 ? 111 GLU A C 1 ATOM 863 O O . GLU A 1 112 ? 46.165 -26.776 19.603 1.00 29.89 ? 111 GLU A O 1 ATOM 864 C CB . GLU A 1 112 ? 47.509 -24.673 21.411 1.00 31.27 ? 111 GLU A CB 1 ATOM 865 C CG . GLU A 1 112 ? 47.761 -23.380 22.114 1.00 40.03 ? 111 GLU A CG 1 ATOM 866 C CD . GLU A 1 112 ? 48.461 -23.586 23.428 1.00 51.61 ? 111 GLU A CD 1 ATOM 867 O OE1 . GLU A 1 112 ? 48.574 -24.756 23.843 1.00 52.11 ? 111 GLU A OE1 1 ATOM 868 O OE2 . GLU A 1 112 ? 48.888 -22.582 24.047 1.00 64.02 ? 111 GLU A OE2 1 ATOM 869 N N . PRO A 1 113 ? 47.895 -26.027 18.407 1.00 32.81 ? 112 PRO A N 1 ATOM 870 C CA . PRO A 1 113 ? 48.131 -27.346 17.821 1.00 32.86 ? 112 PRO A CA 1 ATOM 871 C C . PRO A 1 113 ? 48.757 -28.286 18.840 1.00 36.32 ? 112 PRO A C 1 ATOM 872 O O . PRO A 1 113 ? 49.484 -27.865 19.741 1.00 39.35 ? 112 PRO A O 1 ATOM 873 C CB . PRO A 1 113 ? 49.099 -27.050 16.670 1.00 34.56 ? 112 PRO A CB 1 ATOM 874 C CG . PRO A 1 113 ? 49.820 -25.803 17.108 1.00 28.22 ? 112 PRO A CG 1 ATOM 875 C CD . PRO A 1 113 ? 48.794 -24.998 17.858 1.00 30.41 ? 112 PRO A CD 1 ATOM 876 N N . THR A 1 114 ? 48.445 -29.571 18.696 1.00 33.73 ? 113 THR A N 1 ATOM 877 C CA . THR A 1 114 ? 49.118 -30.632 19.434 1.00 35.35 ? 113 THR A CA 1 ATOM 878 C C . THR A 1 114 ? 50.266 -31.174 18.581 1.00 37.69 ? 113 THR A C 1 ATOM 879 O O . THR A 1 114 ? 50.041 -31.709 17.486 1.00 34.47 ? 113 THR A O 1 ATOM 880 C CB . THR A 1 114 ? 48.121 -31.727 19.807 1.00 37.05 ? 113 THR A CB 1 ATOM 881 O OG1 . THR A 1 114 ? 47.087 -31.152 20.604 1.00 37.20 ? 113 THR A OG1 1 ATOM 882 C CG2 . THR A 1 114 ? 48.788 -32.830 20.605 1.00 35.30 ? 113 THR A CG2 1 ATOM 883 N N . VAL A 1 115 ? 51.495 -31.006 19.067 1.00 36.61 ? 114 VAL A N 1 ATOM 884 C CA . VAL A 1 115 ? 52.697 -31.217 18.266 1.00 34.30 ? 114 VAL A CA 1 ATOM 885 C C . VAL A 1 115 ? 53.379 -32.505 18.712 1.00 35.33 ? 114 VAL A C 1 ATOM 886 O O . VAL A 1 115 ? 53.524 -32.755 19.913 1.00 36.18 ? 114 VAL A O 1 ATOM 887 C CB . VAL A 1 115 ? 53.641 -30.008 18.364 1.00 36.78 ? 114 VAL A CB 1 ATOM 888 C CG1 . VAL A 1 115 ? 54.914 -30.229 17.523 1.00 34.32 ? 114 VAL A CG1 1 ATOM 889 C CG2 . VAL A 1 115 ? 52.886 -28.728 17.926 1.00 33.75 ? 114 VAL A CG2 1 ATOM 890 N N . SER A 1 116 ? 53.767 -33.337 17.746 1.00 34.32 ? 115 SER A N 1 ATOM 891 C CA . SER A 1 116 ? 54.544 -34.537 18.034 1.00 37.87 ? 115 SER A CA 1 ATOM 892 C C . SER A 1 116 ? 55.562 -34.796 16.925 1.00 34.64 ? 115 SER A C 1 ATOM 893 O O . SER A 1 116 ? 55.340 -34.469 15.759 1.00 34.13 ? 115 SER A O 1 ATOM 894 C CB . SER A 1 116 ? 53.637 -35.759 18.211 1.00 32.06 ? 115 SER A CB 1 ATOM 895 O OG . SER A 1 116 ? 52.912 -36.004 17.029 1.00 37.53 ? 115 SER A OG 1 ATOM 896 N N . LEU A 1 117 ? 56.683 -35.399 17.301 1.00 42.99 ? 116 LEU A N 1 ATOM 897 C CA . LEU A 1 117 ? 57.727 -35.775 16.357 1.00 45.00 ? 116 LEU A CA 1 ATOM 898 C C . LEU A 1 117 ? 58.031 -37.255 16.516 1.00 44.90 ? 116 LEU A C 1 ATOM 899 O O . LEU A 1 117 ? 58.214 -37.734 17.641 1.00 41.42 ? 116 LEU A O 1 ATOM 900 C CB . LEU A 1 117 ? 58.992 -34.946 16.578 1.00 48.28 ? 116 LEU A CB 1 ATOM 901 C CG . LEU A 1 117 ? 60.126 -35.123 15.577 1.00 42.21 ? 116 LEU A CG 1 ATOM 902 C CD1 . LEU A 1 117 ? 59.662 -34.751 14.173 1.00 41.56 ? 116 LEU A CD1 1 ATOM 903 C CD2 . LEU A 1 117 ? 61.297 -34.252 16.019 1.00 46.35 ? 116 LEU A CD2 1 ATOM 904 N N . ILE A 1 118 ? 58.078 -37.975 15.390 1.00 46.31 ? 117 ILE A N 1 ATOM 905 C CA . ILE A 1 118 ? 58.373 -39.400 15.385 1.00 50.08 ? 117 ILE A CA 1 ATOM 906 C C . ILE A 1 118 ? 59.465 -39.680 14.368 1.00 51.62 ? 117 ILE A C 1 ATOM 907 O O . ILE A 1 118 ? 59.624 -38.970 13.374 1.00 53.34 ? 117 ILE A O 1 ATOM 908 C CB . ILE A 1 118 ? 57.137 -40.275 15.075 1.00 51.76 ? 117 ILE A CB 1 ATOM 909 C CG1 . ILE A 1 118 ? 56.640 -40.009 13.650 1.00 50.20 ? 117 ILE A CG1 1 ATOM 910 C CG2 . ILE A 1 118 ? 56.055 -40.061 16.134 1.00 44.94 ? 117 ILE A CG2 1 ATOM 911 C CD1 . ILE A 1 118 ? 55.623 -41.026 13.164 1.00 52.34 ? 117 ILE A CD1 1 ATOM 912 N N . LYS A 1 119 ? 60.175 -40.769 14.601 1.00 53.99 ? 118 LYS A N 1 ATOM 913 C CA . LYS A 1 119 ? 61.377 -41.104 13.862 1.00 63.30 ? 118 LYS A CA 1 ATOM 914 C C . LYS A 1 119 ? 61.118 -41.830 12.504 1.00 58.55 ? 118 LYS A C 1 ATOM 915 O O . LYS A 1 119 ? 62.052 -42.230 11.804 1.00 66.73 ? 118 LYS A O 1 ATOM 916 C CB . LYS A 1 119 ? 62.274 -41.860 14.833 1.00 56.82 ? 118 LYS A CB 1 ATOM 917 C CG . LYS A 1 119 ? 63.194 -42.751 14.182 1.00 74.68 ? 118 LYS A CG 1 ATOM 918 C CD . LYS A 1 119 ? 64.390 -42.018 13.697 1.00 71.47 ? 118 LYS A CD 1 ATOM 919 C CE . LYS A 1 119 ? 65.579 -42.928 13.699 1.00 82.96 ? 118 LYS A CE 1 ATOM 920 N NZ . LYS A 1 119 ? 66.880 -42.141 13.876 1.00 77.62 ? 118 LYS A NZ 1 ATOM 921 N N . GLY A 1 120 ? 59.898 -41.866 12.010 1.00 55.09 ? 119 GLY A N 1 ATOM 922 C CA . GLY A 1 120 ? 59.682 -42.410 10.689 1.00 66.09 ? 119 GLY A CA 1 ATOM 923 C C . GLY A 1 120 ? 59.747 -43.925 10.669 1.00 81.17 ? 119 GLY A C 1 ATOM 924 O O . GLY A 1 120 ? 60.422 -44.562 11.490 1.00 74.90 ? 119 GLY A O 1 ATOM 925 N N . PRO A 1 121 ? 59.078 -44.531 9.674 1.00 87.50 ? 120 PRO A N 1 ATOM 926 C CA . PRO A 1 121 ? 58.697 -45.947 9.768 1.00 86.01 ? 120 PRO A CA 1 ATOM 927 C C . PRO A 1 121 ? 59.839 -46.904 9.466 1.00 97.34 ? 120 PRO A C 1 ATOM 928 O O . PRO A 1 121 ? 60.022 -47.917 10.156 1.00 97.08 ? 120 PRO A O 1 ATOM 929 C CB . PRO A 1 121 ? 57.582 -46.058 8.722 1.00 79.48 ? 120 PRO A CB 1 ATOM 930 C CG . PRO A 1 121 ? 58.007 -45.078 7.642 1.00 83.14 ? 120 PRO A CG 1 ATOM 931 C CD . PRO A 1 121 ? 58.780 -43.969 8.340 1.00 80.82 ? 120 PRO A CD 1 ATOM 932 N N . ASP A 1 122 ? 60.599 -46.601 8.420 1.00 93.85 ? 121 ASP A N 1 ATOM 933 C CA . ASP A 1 122 ? 61.676 -47.443 7.929 1.00 91.43 ? 121 ASP A CA 1 ATOM 934 C C . ASP A 1 122 ? 62.979 -47.002 8.570 1.00 94.15 ? 121 ASP A C 1 ATOM 935 O O . ASP A 1 122 ? 63.107 -45.871 9.043 1.00 100.01 ? 121 ASP A O 1 ATOM 936 C CB . ASP A 1 122 ? 61.771 -47.363 6.401 1.00 85.38 ? 121 ASP A CB 1 ATOM 937 C CG . ASP A 1 122 ? 60.597 -48.052 5.697 1.00 88.84 ? 121 ASP A CG 1 ATOM 938 O OD1 . ASP A 1 122 ? 59.961 -48.945 6.309 1.00 83.37 ? 121 ASP A OD1 1 ATOM 939 O OD2 . ASP A 1 122 ? 60.304 -47.695 4.533 1.00 77.64 ? 121 ASP A OD2 1 ATOM 940 N N . SER A 1 123 ? 63.950 -47.906 8.587 1.00 96.10 ? 122 SER A N 1 ATOM 941 C CA . SER A 1 123 ? 65.227 -47.603 9.218 1.00 101.38 ? 122 SER A CA 1 ATOM 942 C C . SER A 1 123 ? 66.228 -47.058 8.199 1.00 103.41 ? 122 SER A C 1 ATOM 943 O O . SER A 1 123 ? 66.118 -47.292 6.991 1.00 108.17 ? 122 SER A O 1 ATOM 944 C CB . SER A 1 123 ? 65.790 -48.835 9.923 1.00 102.58 ? 122 SER A CB 1 ATOM 945 O OG . SER A 1 123 ? 65.164 -49.020 11.183 1.00 105.51 ? 122 SER A OG 1 ATOM 946 N N . LEU A 1 124 ? 67.229 -46.339 8.716 1.00 102.90 ? 123 LEU A N 1 ATOM 947 C CA . LEU A 1 124 ? 68.026 -45.382 7.936 1.00 109.98 ? 123 LEU A CA 1 ATOM 948 C C . LEU A 1 124 ? 69.295 -46.042 7.396 1.00 111.63 ? 123 LEU A C 1 ATOM 949 O O . LEU A 1 124 ? 70.282 -46.191 8.121 1.00 102.61 ? 123 LEU A O 1 ATOM 950 C CB . LEU A 1 124 ? 68.376 -44.166 8.793 1.00 105.58 ? 123 LEU A CB 1 ATOM 951 C CG . LEU A 1 124 ? 67.238 -43.407 9.487 1.00 100.46 ? 123 LEU A CG 1 ATOM 952 C CD1 . LEU A 1 124 ? 67.151 -43.874 10.914 1.00 85.65 ? 123 LEU A CD1 1 ATOM 953 C CD2 . LEU A 1 124 ? 67.431 -41.894 9.437 1.00 84.01 ? 123 LEU A CD2 1 ATOM 954 N N . ILE A 1 125 ? 69.292 -46.391 6.104 1.00 117.90 ? 124 ILE A N 1 ATOM 955 C CA . ILE A 1 125 ? 70.450 -47.056 5.509 1.00 113.37 ? 124 ILE A CA 1 ATOM 956 C C . ILE A 1 125 ? 70.983 -46.272 4.308 1.00 117.05 ? 124 ILE A C 1 ATOM 957 O O . ILE A 1 125 ? 70.241 -45.735 3.479 1.00 120.10 ? 124 ILE A O 1 ATOM 958 C CB . ILE A 1 125 ? 70.173 -48.523 5.108 1.00 116.49 ? 124 ILE A CB 1 ATOM 959 C CG1 . ILE A 1 125 ? 68.970 -48.631 4.167 1.00 111.95 ? 124 ILE A CG1 1 ATOM 960 C CG2 . ILE A 1 125 ? 70.028 -49.399 6.346 1.00 120.21 ? 124 ILE A CG2 1 ATOM 961 C CD1 . ILE A 1 125 ? 69.157 -49.658 3.060 1.00 97.71 ? 124 ILE A CD1 1 ATOM 962 N N . ASP A 1 126 ? 72.295 -46.349 4.176 1.00 112.62 ? 125 ASP A N 1 ATOM 963 C CA . ASP A 1 126 ? 73.182 -45.407 3.532 1.00 107.82 ? 125 ASP A CA 1 ATOM 964 C C . ASP A 1 126 ? 73.200 -45.560 2.012 1.00 107.55 ? 125 ASP A C 1 ATOM 965 O O . ASP A 1 126 ? 72.859 -46.608 1.456 1.00 105.63 ? 125 ASP A O 1 ATOM 966 C CB . ASP A 1 126 ? 74.571 -45.622 4.121 1.00 106.53 ? 125 ASP A CB 1 ATOM 967 C CG . ASP A 1 126 ? 75.426 -44.415 4.049 1.00 106.07 ? 125 ASP A CG 1 ATOM 968 O OD1 . ASP A 1 126 ? 76.521 -44.454 4.617 1.00 114.74 ? 125 ASP A OD1 1 ATOM 969 O OD2 . ASP A 1 126 ? 75.033 -43.431 3.408 1.00 111.17 ? 125 ASP A OD2 1 ATOM 970 N N . GLY A 1 127 ? 73.595 -44.469 1.343 1.00 108.57 ? 126 GLY A N 1 ATOM 971 C CA . GLY A 1 127 ? 73.709 -44.390 -0.099 1.00 102.27 ? 126 GLY A CA 1 ATOM 972 C C . GLY A 1 127 ? 72.432 -44.641 -0.867 1.00 113.01 ? 126 GLY A C 1 ATOM 973 O O . GLY A 1 127 ? 72.457 -44.626 -2.104 1.00 107.78 ? 126 GLY A O 1 ATOM 974 N N . GLY A 1 128 ? 71.311 -44.854 -0.180 1.00 113.36 ? 127 GLY A N 1 ATOM 975 C CA . GLY A 1 128 ? 70.121 -45.380 -0.801 1.00 116.71 ? 127 GLY A CA 1 ATOM 976 C C . GLY A 1 128 ? 69.112 -44.313 -1.182 1.00 114.95 ? 127 GLY A C 1 ATOM 977 O O . GLY A 1 128 ? 69.405 -43.118 -1.266 1.00 112.11 ? 127 GLY A O 1 ATOM 978 N N . ASN A 1 129 ? 67.892 -44.780 -1.425 1.00 110.88 ? 128 ASN A N 1 ATOM 979 C CA . ASN A 1 129 ? 66.806 -43.923 -1.870 1.00 103.21 ? 128 ASN A CA 1 ATOM 980 C C . ASN A 1 129 ? 66.379 -43.005 -0.732 1.00 98.14 ? 128 ASN A C 1 ATOM 981 O O . ASN A 1 129 ? 66.761 -43.203 0.427 1.00 89.52 ? 128 ASN A O 1 ATOM 982 C CB . ASN A 1 129 ? 65.630 -44.781 -2.343 1.00 108.36 ? 128 ASN A CB 1 ATOM 983 C CG . ASN A 1 129 ? 64.837 -44.134 -3.477 1.00 103.01 ? 128 ASN A CG 1 ATOM 984 O OD1 . ASN A 1 129 ? 64.420 -42.978 -3.385 1.00 102.18 ? 128 ASN A OD1 1 ATOM 985 N ND2 . ASN A 1 129 ? 64.629 -44.887 -4.553 1.00 102.58 ? 128 ASN A ND2 1 ATOM 986 N N . GLU A 1 130 ? 65.585 -41.994 -1.064 1.00 97.01 ? 129 GLU A N 1 ATOM 987 C CA . GLU A 1 130 ? 65.062 -41.106 -0.045 1.00 89.19 ? 129 GLU A CA 1 ATOM 988 C C . GLU A 1 130 ? 64.273 -41.901 0.975 1.00 81.54 ? 129 GLU A C 1 ATOM 989 O O . GLU A 1 130 ? 63.579 -42.854 0.627 1.00 73.26 ? 129 GLU A O 1 ATOM 990 C CB . GLU A 1 130 ? 64.162 -40.091 -0.717 1.00 79.72 ? 129 GLU A CB 1 ATOM 991 C CG . GLU A 1 130 ? 63.040 -40.838 -1.488 1.00 83.77 ? 129 GLU A CG 1 ATOM 992 C CD . GLU A 1 130 ? 61.794 -40.042 -1.384 1.00 87.08 ? 129 GLU A CD 1 ATOM 993 O OE1 . GLU A 1 130 ? 60.788 -40.629 -0.873 1.00 95.77 ? 129 GLU A OE1 1 ATOM 994 O OE2 . GLU A 1 130 ? 61.879 -38.926 -1.890 1.00 95.06 ? 129 GLU A OE2 1 ATOM 995 N N . THR A 1 131 ? 64.441 -41.537 2.230 1.00 79.08 ? 130 THR A N 1 ATOM 996 C CA . THR A 1 131 ? 63.791 -42.185 3.340 1.00 68.95 ? 130 THR A CA 1 ATOM 997 C C . THR A 1 131 ? 63.277 -41.095 4.266 1.00 75.97 ? 130 THR A C 1 ATOM 998 O O . THR A 1 131 ? 63.891 -40.027 4.393 1.00 80.82 ? 130 THR A O 1 ATOM 999 C CB . THR A 1 131 ? 64.759 -43.114 4.061 1.00 62.13 ? 130 THR A CB 1 ATOM 1000 N N . VAL A 1 132 ? 62.125 -41.359 4.879 1.00 63.60 ? 131 VAL A N 1 ATOM 1001 C CA . VAL A 1 132 ? 61.508 -40.434 5.821 1.00 58.88 ? 131 VAL A CA 1 ATOM 1002 C C . VAL A 1 132 ? 62.238 -40.569 7.152 1.00 56.59 ? 131 VAL A C 1 ATOM 1003 O O . VAL A 1 132 ? 62.096 -41.571 7.849 1.00 56.89 ? 131 VAL A O 1 ATOM 1004 C CB . VAL A 1 132 ? 60.014 -40.722 5.980 1.00 59.22 ? 131 VAL A CB 1 ATOM 1005 C CG1 . VAL A 1 132 ? 59.399 -39.760 6.993 1.00 58.37 ? 131 VAL A CG1 1 ATOM 1006 C CG2 . VAL A 1 132 ? 59.301 -40.652 4.627 1.00 46.72 ? 131 VAL A CG2 1 ATOM 1007 N N . ALA A 1 133 ? 63.017 -39.550 7.516 1.00 60.43 ? 132 ALA A N 1 ATOM 1008 C CA . ALA A 1 133 ? 63.775 -39.632 8.757 1.00 65.12 ? 132 ALA A CA 1 ATOM 1009 C C . ALA A 1 133 ? 62.924 -39.278 9.963 1.00 57.24 ? 132 ALA A C 1 ATOM 1010 O O . ALA A 1 133 ? 63.155 -39.797 11.061 1.00 59.16 ? 132 ALA A O 1 ATOM 1011 C CB . ALA A 1 133 ? 65.003 -38.718 8.696 1.00 67.40 ? 132 ALA A CB 1 ATOM 1012 N N . ALA A 1 134 ? 61.937 -38.414 9.778 1.00 55.48 ? 133 ALA A N 1 ATOM 1013 C CA . ALA A 1 134 ? 61.120 -37.965 10.887 1.00 54.75 ? 133 ALA A CA 1 ATOM 1014 C C . ALA A 1 134 ? 59.842 -37.375 10.328 1.00 54.75 ? 133 ALA A C 1 ATOM 1015 O O . ALA A 1 134 ? 59.817 -36.868 9.201 1.00 54.11 ? 133 ALA A O 1 ATOM 1016 C CB . ALA A 1 134 ? 61.860 -36.938 11.750 1.00 59.14 ? 133 ALA A CB 1 ATOM 1017 N N . VAL A 1 135 ? 58.781 -37.464 11.127 1.00 55.51 ? 134 VAL A N 1 ATOM 1018 C CA . VAL A 1 135 ? 57.471 -36.907 10.801 1.00 57.17 ? 134 VAL A CA 1 ATOM 1019 C C . VAL A 1 135 ? 57.098 -35.955 11.924 1.00 51.85 ? 134 VAL A C 1 ATOM 1020 O O . VAL A 1 135 ? 57.127 -36.340 13.100 1.00 49.56 ? 134 VAL A O 1 ATOM 1021 C CB . VAL A 1 135 ? 56.398 -38.003 10.634 1.00 59.01 ? 134 VAL A CB 1 ATOM 1022 C CG1 . VAL A 1 135 ? 55.052 -37.399 10.228 1.00 50.66 ? 134 VAL A CG1 1 ATOM 1023 C CG2 . VAL A 1 135 ? 56.844 -39.036 9.620 1.00 62.30 ? 134 VAL A CG2 1 ATOM 1024 N N . CYS A 1 136 ? 56.771 -34.713 11.565 1.00 49.90 ? 135 CYS A N 1 ATOM 1025 C CA . CYS A 1 136 ? 56.302 -33.712 12.514 1.00 46.15 ? 135 CYS A CA 1 ATOM 1026 C C . CYS A 1 136 ? 54.834 -33.409 12.238 1.00 45.41 ? 135 CYS A C 1 ATOM 1027 O O . CYS A 1 136 ? 54.451 -33.145 11.090 1.00 41.98 ? 135 CYS A O 1 ATOM 1028 C CB . CYS A 1 136 ? 57.139 -32.428 12.431 1.00 44.26 ? 135 CYS A CB 1 ATOM 1029 S SG . CYS A 1 136 ? 56.962 -31.264 13.858 1.00 45.35 ? 135 CYS A SG 1 ATOM 1030 N N . VAL A 1 137 ? 54.017 -33.449 13.289 1.00 41.82 ? 136 VAL A N 1 ATOM 1031 C CA . VAL A 1 137 ? 52.581 -33.225 13.181 1.00 34.48 ? 136 VAL A CA 1 ATOM 1032 C C . VAL A 1 137 ? 52.207 -32.136 14.167 1.00 40.21 ? 136 VAL A C 1 ATOM 1033 O O . VAL A 1 137 ? 52.506 -32.248 15.362 1.00 40.71 ? 136 VAL A O 1 ATOM 1034 C CB . VAL A 1 137 ? 51.763 -34.502 13.475 1.00 45.18 ? 136 VAL A CB 1 ATOM 1035 C CG1 . VAL A 1 137 ? 50.263 -34.237 13.278 1.00 36.63 ? 136 VAL A CG1 1 ATOM 1036 C CG2 . VAL A 1 137 ? 52.241 -35.698 12.636 1.00 43.72 ? 136 VAL A CG2 1 ATOM 1037 N N . ALA A 1 138 ? 51.565 -31.087 13.669 1.00 38.29 ? 137 ALA A N 1 ATOM 1038 C CA . ALA A 1 138 ? 50.932 -30.065 14.497 1.00 39.84 ? 137 ALA A CA 1 ATOM 1039 C C . ALA A 1 138 ? 49.419 -30.191 14.273 1.00 33.84 ? 137 ALA A C 1 ATOM 1040 O O . ALA A 1 138 ? 48.880 -29.704 13.275 1.00 32.51 ? 137 ALA A O 1 ATOM 1041 C CB . ALA A 1 138 ? 51.481 -28.680 14.144 1.00 35.15 ? 137 ALA A CB 1 ATOM 1042 N N . ALA A 1 139 ? 48.735 -30.869 15.185 1.00 37.78 ? 138 ALA A N 1 ATOM 1043 C CA . ALA A 1 139 ? 47.375 -31.335 14.927 1.00 32.59 ? 138 ALA A CA 1 ATOM 1044 C C . ALA A 1 139 ? 46.329 -30.375 15.469 1.00 32.95 ? 138 ALA A C 1 ATOM 1045 O O . ALA A 1 139 ? 46.483 -29.821 16.563 1.00 32.39 ? 138 ALA A O 1 ATOM 1046 C CB . ALA A 1 139 ? 47.149 -32.717 15.544 1.00 30.86 ? 138 ALA A CB 1 ATOM 1047 N N . THR A 1 140 ? 45.263 -30.203 14.684 1.00 41.90 ? 139 THR A N 1 ATOM 1048 C CA . THR A 1 140 ? 44.021 -29.500 15.042 1.00 33.63 ? 139 THR A CA 1 ATOM 1049 C C . THR A 1 140 ? 44.296 -28.186 15.760 1.00 32.12 ? 139 THR A C 1 ATOM 1050 O O . THR A 1 140 ? 43.837 -27.935 16.874 1.00 32.06 ? 139 THR A O 1 ATOM 1051 C CB . THR A 1 140 ? 43.087 -30.391 15.862 1.00 30.12 ? 139 THR A CB 1 ATOM 1052 O OG1 . THR A 1 140 ? 43.841 -31.161 16.804 1.00 33.22 ? 139 THR A OG1 1 ATOM 1053 C CG2 . THR A 1 140 ? 42.322 -31.332 14.964 1.00 34.21 ? 139 THR A CG2 1 ATOM 1054 N N . GLY A 1 141 ? 45.048 -27.330 15.081 1.00 34.59 ? 140 GLY A N 1 ATOM 1055 C CA . GLY A 1 141 ? 45.326 -25.990 15.555 1.00 31.42 ? 140 GLY A CA 1 ATOM 1056 C C . GLY A 1 141 ? 44.524 -25.003 14.735 1.00 30.34 ? 140 GLY A C 1 ATOM 1057 O O . GLY A 1 141 ? 44.176 -25.273 13.591 1.00 31.52 ? 140 GLY A O 1 ATOM 1058 N N . LYS A 1 142 ? 44.235 -23.855 15.321 1.00 31.30 ? 141 LYS A N 1 ATOM 1059 C CA . LYS A 1 142 ? 43.446 -22.866 14.623 1.00 30.37 ? 141 LYS A CA 1 ATOM 1060 C C . LYS A 1 142 ? 44.139 -21.530 14.780 1.00 30.51 ? 141 LYS A C 1 ATOM 1061 O O . LYS A 1 142 ? 44.259 -21.029 15.892 1.00 29.24 ? 141 LYS A O 1 ATOM 1062 C CB . LYS A 1 142 ? 42.007 -22.813 15.160 1.00 32.12 ? 141 LYS A CB 1 ATOM 1063 C CG . LYS A 1 142 ? 41.091 -21.855 14.380 1.00 28.54 ? 141 LYS A CG 1 ATOM 1064 C CD . LYS A 1 142 ? 39.719 -21.754 15.012 1.00 30.59 ? 141 LYS A CD 1 ATOM 1065 C CE . LYS A 1 142 ? 38.910 -20.616 14.419 1.00 29.86 ? 141 LYS A CE 1 ATOM 1066 N NZ . LYS A 1 142 ? 39.489 -19.280 14.692 1.00 33.68 ? 141 LYS A NZ 1 ATOM 1067 N N . PRO A 1 143 ? 44.625 -20.967 13.666 1.00 30.02 ? 142 PRO A N 1 ATOM 1068 C CA . PRO A 1 143 ? 44.595 -21.590 12.334 1.00 29.49 ? 142 PRO A CA 1 ATOM 1069 C C . PRO A 1 143 ? 45.655 -22.686 12.195 1.00 34.25 ? 142 PRO A C 1 ATOM 1070 O O . PRO A 1 143 ? 46.167 -23.131 13.223 1.00 34.80 ? 142 PRO A O 1 ATOM 1071 C CB . PRO A 1 143 ? 44.889 -20.426 11.404 1.00 22.26 ? 142 PRO A CB 1 ATOM 1072 C CG . PRO A 1 143 ? 45.757 -19.544 12.216 1.00 35.67 ? 142 PRO A CG 1 ATOM 1073 C CD . PRO A 1 143 ? 45.256 -19.641 13.631 1.00 33.69 ? 142 PRO A CD 1 ATOM 1074 N N . VAL A 1 144 ? 45.969 -23.130 10.974 1.00 30.38 ? 143 VAL A N 1 ATOM 1075 C CA . VAL A 1 144 ? 46.936 -24.211 10.814 1.00 34.16 ? 143 VAL A CA 1 ATOM 1076 C C . VAL A 1 144 ? 48.334 -23.688 11.151 1.00 29.22 ? 143 VAL A C 1 ATOM 1077 O O . VAL A 1 144 ? 48.697 -22.541 10.842 1.00 30.36 ? 143 VAL A O 1 ATOM 1078 C CB . VAL A 1 144 ? 46.852 -24.806 9.390 1.00 25.11 ? 143 VAL A CB 1 ATOM 1079 C CG1 . VAL A 1 144 ? 47.276 -23.797 8.366 1.00 23.68 ? 143 VAL A CG1 1 ATOM 1080 C CG2 . VAL A 1 144 ? 47.681 -26.063 9.250 1.00 27.40 ? 143 VAL A CG2 1 ATOM 1081 N N . ALA A 1 145 ? 49.111 -24.504 11.844 1.00 27.20 ? 144 ALA A N 1 ATOM 1082 C CA . ALA A 1 145 ? 50.489 -24.118 12.117 1.00 39.31 ? 144 ALA A CA 1 ATOM 1083 C C . ALA A 1 145 ? 51.337 -24.129 10.831 1.00 34.73 ? 144 ALA A C 1 ATOM 1084 O O . ALA A 1 145 ? 50.924 -24.594 9.760 1.00 31.79 ? 144 ALA A O 1 ATOM 1085 C CB . ALA A 1 145 ? 51.110 -25.045 13.168 1.00 35.72 ? 144 ALA A CB 1 ATOM 1086 N N . GLN A 1 146 ? 52.534 -23.576 10.952 1.00 34.70 ? 145 GLN A N 1 ATOM 1087 C CA . GLN A 1 146 ? 53.590 -23.756 9.967 1.00 38.26 ? 145 GLN A CA 1 ATOM 1088 C C . GLN A 1 146 ? 54.686 -24.611 10.570 1.00 33.79 ? 145 GLN A C 1 ATOM 1089 O O . GLN A 1 146 ? 55.003 -24.490 11.757 1.00 32.27 ? 145 GLN A O 1 ATOM 1090 C CB . GLN A 1 146 ? 54.150 -22.418 9.490 1.00 31.80 ? 145 GLN A CB 1 ATOM 1091 C CG . GLN A 1 146 ? 53.073 -21.480 9.016 1.00 33.37 ? 145 GLN A CG 1 ATOM 1092 C CD . GLN A 1 146 ? 53.579 -20.090 8.704 1.00 56.07 ? 145 GLN A CD 1 ATOM 1093 O OE1 . GLN A 1 146 ? 52.930 -19.349 7.984 1.00 66.58 ? 145 GLN A OE1 1 ATOM 1094 N NE2 . GLN A 1 146 ? 54.737 -19.729 9.236 1.00 46.59 ? 145 GLN A NE2 1 ATOM 1095 N N . ILE A 1 147 ? 55.229 -25.510 9.762 1.00 37.56 ? 146 ILE A N 1 ATOM 1096 C CA . ILE A 1 147 ? 56.316 -26.382 10.178 1.00 41.05 ? 146 ILE A CA 1 ATOM 1097 C C . ILE A 1 147 ? 57.534 -26.103 9.314 1.00 46.16 ? 146 ILE A C 1 ATOM 1098 O O . ILE A 1 147 ? 57.460 -26.177 8.081 1.00 45.87 ? 146 ILE A O 1 ATOM 1099 C CB . ILE A 1 147 ? 55.935 -27.862 10.079 1.00 44.83 ? 146 ILE A CB 1 ATOM 1100 C CG1 . ILE A 1 147 ? 54.794 -28.189 11.044 1.00 34.43 ? 146 ILE A CG1 1 ATOM 1101 C CG2 . ILE A 1 147 ? 57.193 -28.714 10.315 1.00 36.90 ? 146 ILE A CG2 1 ATOM 1102 C CD1 . ILE A 1 147 ? 54.260 -29.600 10.849 1.00 39.56 ? 146 ILE A CD1 1 ATOM 1103 N N . ASP A 1 148 ? 58.651 -25.807 9.971 1.00 49.05 ? 147 ASP A N 1 ATOM 1104 C CA . ASP A 1 148 ? 59.955 -25.608 9.362 1.00 43.55 ? 147 ASP A CA 1 ATOM 1105 C C . ASP A 1 148 ? 60.951 -26.585 9.990 1.00 46.29 ? 147 ASP A C 1 ATOM 1106 O O . ASP A 1 148 ? 60.741 -27.104 11.092 1.00 42.74 ? 147 ASP A O 1 ATOM 1107 C CB . ASP A 1 148 ? 60.414 -24.152 9.556 1.00 51.58 ? 147 ASP A CB 1 ATOM 1108 C CG . ASP A 1 148 ? 61.377 -23.690 8.489 1.00 58.31 ? 147 ASP A CG 1 ATOM 1109 O OD1 . ASP A 1 148 ? 61.933 -24.551 7.768 1.00 60.21 ? 147 ASP A OD1 1 ATOM 1110 O OD2 . ASP A 1 148 ? 61.579 -22.458 8.383 1.00 63.87 ? 147 ASP A OD2 1 ATOM 1111 N N . TRP A 1 149 ? 62.051 -26.840 9.294 1.00 49.53 ? 148 TRP A N 1 ATOM 1112 C CA . TRP A 1 149 ? 63.051 -27.768 9.797 1.00 53.63 ? 148 TRP A CA 1 ATOM 1113 C C . TRP A 1 149 ? 64.423 -27.110 9.897 1.00 49.84 ? 148 TRP A C 1 ATOM 1114 O O . TRP A 1 149 ? 64.801 -26.301 9.047 1.00 56.90 ? 148 TRP A O 1 ATOM 1115 C CB . TRP A 1 149 ? 63.124 -28.995 8.913 1.00 52.62 ? 148 TRP A CB 1 ATOM 1116 C CG . TRP A 1 149 ? 61.874 -29.827 8.938 1.00 52.89 ? 148 TRP A CG 1 ATOM 1117 C CD1 . TRP A 1 149 ? 60.757 -29.656 8.175 1.00 51.79 ? 148 TRP A CD1 1 ATOM 1118 C CD2 . TRP A 1 149 ? 61.632 -30.984 9.750 1.00 57.19 ? 148 TRP A CD2 1 ATOM 1119 N NE1 . TRP A 1 149 ? 59.830 -30.630 8.467 1.00 55.28 ? 148 TRP A NE1 1 ATOM 1120 C CE2 . TRP A 1 149 ? 60.346 -31.461 9.427 1.00 51.81 ? 148 TRP A CE2 1 ATOM 1121 C CE3 . TRP A 1 149 ? 62.382 -31.663 10.720 1.00 56.87 ? 148 TRP A CE3 1 ATOM 1122 C CZ2 . TRP A 1 149 ? 59.793 -32.584 10.033 1.00 48.25 ? 148 TRP A CZ2 1 ATOM 1123 C CZ3 . TRP A 1 149 ? 61.828 -32.770 11.329 1.00 57.29 ? 148 TRP A CZ3 1 ATOM 1124 C CH2 . TRP A 1 149 ? 60.541 -33.220 10.983 1.00 56.37 ? 148 TRP A CH2 1 ATOM 1125 N N . GLU A 1 150 ? 65.164 -27.462 10.944 1.00 45.69 ? 149 GLU A N 1 ATOM 1126 C CA . GLU A 1 150 ? 66.537 -27.016 11.134 1.00 55.65 ? 149 GLU A CA 1 ATOM 1127 C C . GLU A 1 150 ? 67.487 -28.209 11.155 1.00 63.21 ? 149 GLU A C 1 ATOM 1128 O O . GLU A 1 150 ? 67.160 -29.282 11.672 1.00 59.98 ? 149 GLU A O 1 ATOM 1129 C CB . GLU A 1 150 ? 66.681 -26.206 12.424 1.00 39.94 ? 149 GLU A CB 1 ATOM 1130 C CG . GLU A 1 150 ? 65.934 -24.891 12.353 1.00 41.05 ? 149 GLU A CG 1 ATOM 1131 C CD . GLU A 1 150 ? 66.029 -24.117 13.632 1.00 46.30 ? 149 GLU A CD 1 ATOM 1132 O OE1 . GLU A 1 150 ? 66.341 -24.735 14.675 1.00 46.52 ? 149 GLU A OE1 1 ATOM 1133 O OE2 . GLU A 1 150 ? 65.816 -22.889 13.585 1.00 50.05 ? 149 GLU A OE2 1 ATOM 1134 N N . GLY A 1 151 ? 68.686 -27.992 10.620 1.00 76.83 ? 150 GLY A N 1 ATOM 1135 C CA . GLY A 1 151 ? 69.581 -29.073 10.250 1.00 68.60 ? 150 GLY A CA 1 ATOM 1136 C C . GLY A 1 151 ? 69.361 -29.327 8.776 1.00 70.18 ? 150 GLY A C 1 ATOM 1137 O O . GLY A 1 151 ? 68.267 -29.742 8.383 1.00 75.54 ? 150 GLY A O 1 ATOM 1138 N N . ASP A 1 152 ? 70.363 -29.038 7.945 1.00 62.66 ? 151 ASP A N 1 ATOM 1139 C CA . ASP A 1 152 ? 70.185 -29.016 6.491 1.00 67.02 ? 151 ASP A CA 1 ATOM 1140 C C . ASP A 1 152 ? 70.649 -30.352 5.918 1.00 75.03 ? 151 ASP A C 1 ATOM 1141 O O . ASP A 1 152 ? 71.750 -30.489 5.381 1.00 70.85 ? 151 ASP A O 1 ATOM 1142 C CB . ASP A 1 152 ? 70.947 -27.849 5.868 1.00 77.38 ? 151 ASP A CB 1 ATOM 1143 C CG . ASP A 1 152 ? 70.354 -26.493 6.225 1.00 76.48 ? 151 ASP A CG 1 ATOM 1144 O OD1 . ASP A 1 152 ? 69.176 -26.425 6.630 1.00 78.02 ? 151 ASP A OD1 1 ATOM 1145 O OD2 . ASP A 1 152 ? 71.073 -25.480 6.085 1.00 92.46 ? 151 ASP A OD2 1 ATOM 1146 N N . LEU A 1 153 ? 69.781 -31.355 6.033 1.00 75.02 ? 152 LEU A N 1 ATOM 1147 C CA . LEU A 1 153 ? 70.102 -32.694 5.572 1.00 62.80 ? 152 LEU A CA 1 ATOM 1148 C C . LEU A 1 153 ? 69.113 -33.238 4.552 1.00 65.85 ? 152 LEU A C 1 ATOM 1149 O O . LEU A 1 153 ? 69.265 -34.385 4.130 1.00 70.98 ? 152 LEU A O 1 ATOM 1150 C CB . LEU A 1 153 ? 70.198 -33.654 6.763 1.00 64.38 ? 152 LEU A CB 1 ATOM 1151 C CG . LEU A 1 153 ? 70.911 -33.116 8.011 1.00 76.96 ? 152 LEU A CG 1 ATOM 1152 C CD1 . LEU A 1 153 ? 70.917 -34.140 9.133 1.00 68.93 ? 152 LEU A CD1 1 ATOM 1153 C CD2 . LEU A 1 153 ? 72.333 -32.649 7.717 1.00 83.00 ? 152 LEU A CD2 1 ATOM 1154 N N . GLY A 1 154 ? 68.124 -32.459 4.133 1.00 70.75 ? 153 GLY A N 1 ATOM 1155 C CA . GLY A 1 154 ? 67.180 -32.941 3.144 1.00 69.03 ? 153 GLY A CA 1 ATOM 1156 C C . GLY A 1 154 ? 66.060 -31.955 2.894 1.00 71.35 ? 153 GLY A C 1 ATOM 1157 O O . GLY A 1 154 ? 66.157 -30.774 3.236 1.00 69.59 ? 153 GLY A O 1 ATOM 1158 N N . GLU A 1 155 ? 64.989 -32.458 2.290 1.00 68.96 ? 154 GLU A N 1 ATOM 1159 C CA . GLU A 1 155 ? 63.836 -31.656 1.918 1.00 66.70 ? 154 GLU A CA 1 ATOM 1160 C C . GLU A 1 155 ? 62.613 -32.152 2.682 1.00 68.01 ? 154 GLU A C 1 ATOM 1161 O O . GLU A 1 155 ? 62.601 -33.262 3.221 1.00 67.60 ? 154 GLU A O 1 ATOM 1162 C CB . GLU A 1 155 ? 63.614 -31.727 0.402 1.00 68.99 ? 154 GLU A CB 1 ATOM 1163 C CG . GLU A 1 155 ? 62.650 -30.711 -0.178 1.00 75.46 ? 154 GLU A CG 1 ATOM 1164 C CD . GLU A 1 155 ? 62.248 -31.071 -1.594 1.00 86.14 ? 154 GLU A CD 1 ATOM 1165 O OE1 . GLU A 1 155 ? 61.037 -31.062 -1.897 1.00 78.62 ? 154 GLU A OE1 1 ATOM 1166 O OE2 . GLU A 1 155 ? 63.150 -31.376 -2.404 1.00 102.50 ? 154 GLU A OE2 1 ATOM 1167 N N . MET A 1 156 ? 61.578 -31.326 2.745 1.00 71.77 ? 155 MET A N 1 ATOM 1168 C CA . MET A 1 156 ? 60.361 -31.722 3.437 1.00 71.73 ? 155 MET A CA 1 ATOM 1169 C C . MET A 1 156 ? 59.178 -31.796 2.477 1.00 72.30 ? 155 MET A C 1 ATOM 1170 O O . MET A 1 156 ? 59.178 -31.196 1.400 1.00 72.13 ? 155 MET A O 1 ATOM 1171 C CB . MET A 1 156 ? 60.044 -30.761 4.586 1.00 67.54 ? 155 MET A CB 1 ATOM 1172 C CG . MET A 1 156 ? 59.879 -29.327 4.160 1.00 70.86 ? 155 MET A CG 1 ATOM 1173 S SD . MET A 1 156 ? 58.356 -28.677 4.853 1.00 87.67 ? 155 MET A SD 1 ATOM 1174 C CE . MET A 1 156 ? 57.157 -29.434 3.769 1.00 55.68 ? 155 MET A CE 1 ATOM 1175 N N . GLU A 1 157 ? 58.164 -32.558 2.889 1.00 77.58 ? 156 GLU A N 1 ATOM 1176 C CA . GLU A 1 157 ? 56.888 -32.667 2.190 1.00 73.52 ? 156 GLU A CA 1 ATOM 1177 C C . GLU A 1 157 ? 55.787 -32.605 3.233 1.00 66.62 ? 156 GLU A C 1 ATOM 1178 O O . GLU A 1 157 ? 55.879 -33.286 4.259 1.00 65.21 ? 156 GLU A O 1 ATOM 1179 C CB . GLU A 1 157 ? 56.786 -33.978 1.404 1.00 72.08 ? 156 GLU A CB 1 ATOM 1180 C CG . GLU A 1 157 ? 56.861 -33.814 -0.099 1.00 84.07 ? 156 GLU A CG 1 ATOM 1181 C CD . GLU A 1 157 ? 56.598 -35.119 -0.828 1.00 83.32 ? 156 GLU A CD 1 ATOM 1182 O OE1 . GLU A 1 157 ? 55.826 -35.945 -0.306 1.00 85.05 ? 156 GLU A OE1 1 ATOM 1183 O OE2 . GLU A 1 157 ? 57.176 -35.334 -1.913 1.00 88.25 ? 156 GLU A OE2 1 ATOM 1184 N N . SER A 1 158 ? 54.753 -31.802 2.983 1.00 61.00 ? 157 SER A N 1 ATOM 1185 C CA . SER A 1 158 ? 53.716 -31.599 3.983 1.00 58.52 ? 157 SER A CA 1 ATOM 1186 C C . SER A 1 158 ? 52.335 -31.582 3.345 1.00 64.79 ? 157 SER A C 1 ATOM 1187 O O . SER A 1 158 ? 52.168 -31.187 2.186 1.00 70.95 ? 157 SER A O 1 ATOM 1188 C CB . SER A 1 158 ? 53.909 -30.286 4.748 1.00 61.33 ? 157 SER A CB 1 ATOM 1189 O OG . SER A 1 158 ? 53.430 -29.199 3.978 1.00 55.94 ? 157 SER A OG 1 ATOM 1190 N N . SER A 1 159 ? 51.340 -31.976 4.142 1.00 66.45 ? 158 SER A N 1 ATOM 1191 C CA . SER A 1 159 ? 49.938 -31.958 3.746 1.00 65.38 ? 158 SER A CA 1 ATOM 1192 C C . SER A 1 159 ? 49.112 -31.365 4.877 1.00 57.92 ? 158 SER A C 1 ATOM 1193 O O . SER A 1 159 ? 49.505 -31.418 6.045 1.00 58.83 ? 158 SER A O 1 ATOM 1194 C CB . SER A 1 159 ? 49.415 -33.363 3.388 1.00 54.66 ? 158 SER A CB 1 ATOM 1195 O OG . SER A 1 159 ? 49.426 -34.230 4.502 1.00 51.32 ? 158 SER A OG 1 ATOM 1196 N N . THR A 1 160 ? 47.960 -30.804 4.511 1.00 58.90 ? 159 THR A N 1 ATOM 1197 C CA . THR A 1 160 ? 47.058 -30.130 5.436 1.00 49.41 ? 159 THR A CA 1 ATOM 1198 C C . THR A 1 160 ? 45.661 -30.705 5.272 1.00 51.40 ? 159 THR A C 1 ATOM 1199 O O . THR A 1 160 ? 45.183 -30.844 4.142 1.00 50.53 ? 159 THR A O 1 ATOM 1200 C CB . THR A 1 160 ? 47.030 -28.625 5.171 1.00 51.05 ? 159 THR A CB 1 ATOM 1201 O OG1 . THR A 1 160 ? 48.363 -28.101 5.241 1.00 55.75 ? 159 THR A OG1 1 ATOM 1202 C CG2 . THR A 1 160 ? 46.164 -27.932 6.195 1.00 45.51 ? 159 THR A CG2 1 ATOM 1203 N N . THR A 1 161 ? 45.007 -31.027 6.394 1.00 49.91 ? 160 THR A N 1 ATOM 1204 C CA . THR A 1 161 ? 43.643 -31.563 6.401 1.00 51.97 ? 160 THR A CA 1 ATOM 1205 C C . THR A 1 161 ? 42.765 -30.730 7.338 1.00 47.82 ? 160 THR A C 1 ATOM 1206 O O . THR A 1 161 ? 42.944 -30.766 8.559 1.00 43.36 ? 160 THR A O 1 ATOM 1207 C CB . THR A 1 161 ? 43.642 -33.037 6.810 1.00 49.64 ? 160 THR A CB 1 ATOM 1208 O OG1 . THR A 1 161 ? 44.182 -33.159 8.126 1.00 61.07 ? 160 THR A OG1 1 ATOM 1209 C CG2 . THR A 1 161 ? 44.514 -33.853 5.872 1.00 49.35 ? 160 THR A CG2 1 ATOM 1210 N N . SER A 1 162 ? 41.808 -29.991 6.776 1.00 45.09 ? 161 SER A N 1 ATOM 1211 C CA . SER A 1 162 ? 40.911 -29.132 7.539 1.00 38.64 ? 161 SER A CA 1 ATOM 1212 C C . SER A 1 162 ? 39.728 -29.917 8.122 1.00 39.41 ? 161 SER A C 1 ATOM 1213 O O . SER A 1 162 ? 39.396 -31.012 7.673 1.00 41.53 ? 161 SER A O 1 ATOM 1214 C CB . SER A 1 162 ? 40.398 -28.006 6.653 1.00 41.43 ? 161 SER A CB 1 ATOM 1215 O OG . SER A 1 162 ? 41.481 -27.402 5.977 1.00 64.14 ? 161 SER A OG 1 ATOM 1216 N N . PHE A 1 163 ? 39.082 -29.322 9.121 1.00 40.67 ? 162 PHE A N 1 ATOM 1217 C CA . PHE A 1 163 ? 38.026 -29.932 9.915 1.00 41.70 ? 162 PHE A CA 1 ATOM 1218 C C . PHE A 1 163 ? 36.856 -28.975 10.094 1.00 43.58 ? 162 PHE A C 1 ATOM 1219 O O . PHE A 1 163 ? 36.993 -27.767 9.874 1.00 40.34 ? 162 PHE A O 1 ATOM 1220 C CB . PHE A 1 163 ? 38.556 -30.366 11.289 1.00 36.72 ? 162 PHE A CB 1 ATOM 1221 C CG . PHE A 1 163 ? 39.618 -31.409 11.215 1.00 44.00 ? 162 PHE A CG 1 ATOM 1222 C CD1 . PHE A 1 163 ? 39.293 -32.720 10.893 1.00 39.76 ? 162 PHE A CD1 1 ATOM 1223 C CD2 . PHE A 1 163 ? 40.948 -31.083 11.464 1.00 35.28 ? 162 PHE A CD2 1 ATOM 1224 C CE1 . PHE A 1 163 ? 40.271 -33.691 10.827 1.00 35.03 ? 162 PHE A CE1 1 ATOM 1225 C CE2 . PHE A 1 163 ? 41.928 -32.044 11.405 1.00 30.08 ? 162 PHE A CE2 1 ATOM 1226 C CZ . PHE A 1 163 ? 41.598 -33.343 11.089 1.00 38.48 ? 162 PHE A CZ 1 ATOM 1227 N N . PRO A 1 164 ? 35.677 -29.489 10.478 1.00 50.11 ? 163 PRO A N 1 ATOM 1228 C CA . PRO A 1 164 ? 34.489 -28.616 10.500 1.00 52.32 ? 163 PRO A CA 1 ATOM 1229 C C . PRO A 1 164 ? 34.560 -27.533 11.560 1.00 47.15 ? 163 PRO A C 1 ATOM 1230 O O . PRO A 1 164 ? 34.010 -26.444 11.345 1.00 47.49 ? 163 PRO A O 1 ATOM 1231 C CB . PRO A 1 164 ? 33.328 -29.591 10.770 1.00 47.10 ? 163 PRO A CB 1 ATOM 1232 C CG . PRO A 1 164 ? 33.865 -30.951 10.466 1.00 44.33 ? 163 PRO A CG 1 ATOM 1233 C CD . PRO A 1 164 ? 35.328 -30.893 10.783 1.00 40.69 ? 163 PRO A CD 1 ATOM 1234 N N . ASN A 1 165 ? 35.213 -27.798 12.700 1.00 38.13 ? 164 ASN A N 1 ATOM 1235 C CA . ASN A 1 165 ? 35.325 -26.808 13.764 1.00 36.48 ? 164 ASN A CA 1 ATOM 1236 C C . ASN A 1 165 ? 36.368 -25.735 13.467 1.00 42.39 ? 164 ASN A C 1 ATOM 1237 O O . ASN A 1 165 ? 36.611 -24.872 14.326 1.00 43.67 ? 164 ASN A O 1 ATOM 1238 C CB . ASN A 1 165 ? 35.642 -27.465 15.114 1.00 29.39 ? 164 ASN A CB 1 ATOM 1239 C CG . ASN A 1 165 ? 36.940 -28.265 15.099 1.00 32.33 ? 164 ASN A CG 1 ATOM 1240 O OD1 . ASN A 1 165 ? 37.733 -28.135 14.168 1.00 34.28 ? 164 ASN A OD1 1 ATOM 1241 N ND2 . ASN A 1 165 ? 37.181 -29.069 16.154 1.00 30.52 ? 164 ASN A ND2 1 ATOM 1242 N N . GLU A 1 166 ? 36.977 -25.778 12.278 1.00 42.08 ? 165 GLU A N 1 ATOM 1243 C CA . GLU A 1 166 ? 37.894 -24.764 11.767 1.00 37.60 ? 165 GLU A CA 1 ATOM 1244 C C . GLU A 1 166 ? 39.278 -24.857 12.381 1.00 36.55 ? 165 GLU A C 1 ATOM 1245 O O . GLU A 1 166 ? 40.010 -23.870 12.404 1.00 37.63 ? 165 GLU A O 1 ATOM 1246 C CB . GLU A 1 166 ? 37.341 -23.349 11.942 1.00 34.08 ? 165 GLU A CB 1 ATOM 1247 C CG . GLU A 1 166 ? 36.179 -23.062 11.062 1.00 33.27 ? 165 GLU A CG 1 ATOM 1248 C CD . GLU A 1 166 ? 35.656 -21.675 11.251 1.00 47.89 ? 165 GLU A CD 1 ATOM 1249 O OE1 . GLU A 1 166 ? 34.436 -21.552 11.494 1.00 60.59 ? 165 GLU A OE1 1 ATOM 1250 O OE2 . GLU A 1 166 ? 36.454 -20.713 11.148 1.00 43.04 ? 165 GLU A OE2 1 ATOM 1251 N N . THR A 1 167 ? 39.648 -26.033 12.875 1.00 37.60 ? 166 THR A N 1 ATOM 1252 C CA . THR A 1 167 ? 41.022 -26.380 13.183 1.00 30.75 ? 166 THR A CA 1 ATOM 1253 C C . THR A 1 167 ? 41.585 -27.231 12.055 1.00 39.34 ? 166 THR A C 1 ATOM 1254 O O . THR A 1 167 ? 40.844 -27.888 11.323 1.00 38.77 ? 166 THR A O 1 ATOM 1255 C CB . THR A 1 167 ? 41.104 -27.131 14.500 1.00 30.61 ? 166 THR A CB 1 ATOM 1256 O OG1 . THR A 1 167 ? 40.408 -28.374 14.373 1.00 32.28 ? 166 THR A OG1 1 ATOM 1257 C CG2 . THR A 1 167 ? 40.466 -26.300 15.611 1.00 33.37 ? 166 THR A CG2 1 ATOM 1258 N N . ALA A 1 168 ? 42.901 -27.198 11.894 1.00 37.87 ? 167 ALA A N 1 ATOM 1259 C CA . ALA A 1 168 ? 43.517 -27.909 10.791 1.00 33.13 ? 167 ALA A CA 1 ATOM 1260 C C . ALA A 1 168 ? 44.731 -28.648 11.301 1.00 36.82 ? 167 ALA A C 1 ATOM 1261 O O . ALA A 1 168 ? 45.420 -28.180 12.217 1.00 36.85 ? 167 ALA A O 1 ATOM 1262 C CB . ALA A 1 168 ? 43.921 -26.973 9.657 1.00 34.39 ? 167 ALA A CB 1 ATOM 1263 N N . THR A 1 169 ? 44.970 -29.813 10.705 1.00 37.06 ? 168 THR A N 1 ATOM 1264 C CA . THR A 1 169 ? 46.150 -30.624 10.971 1.00 37.54 ? 168 THR A CA 1 ATOM 1265 C C . THR A 1 169 ? 47.096 -30.540 9.784 1.00 44.05 ? 168 THR A C 1 ATOM 1266 O O . THR A 1 169 ? 46.658 -30.609 8.630 1.00 45.51 ? 168 THR A O 1 ATOM 1267 C CB . THR A 1 169 ? 45.782 -32.078 11.249 1.00 30.88 ? 168 THR A CB 1 ATOM 1268 O OG1 . THR A 1 169 ? 45.192 -32.166 12.544 1.00 34.00 ? 168 THR A OG1 1 ATOM 1269 C CG2 . THR A 1 169 ? 47.002 -32.947 11.218 1.00 36.99 ? 168 THR A CG2 1 ATOM 1270 N N . ILE A 1 170 ? 48.383 -30.343 10.075 1.00 46.08 ? 169 ILE A N 1 ATOM 1271 C CA . ILE A 1 170 ? 49.438 -30.327 9.072 1.00 46.11 ? 169 ILE A CA 1 ATOM 1272 C C . ILE A 1 170 ? 50.467 -31.364 9.482 1.00 47.93 ? 169 ILE A C 1 ATOM 1273 O O . ILE A 1 170 ? 50.882 -31.410 10.649 1.00 46.58 ? 169 ILE A O 1 ATOM 1274 C CB . ILE A 1 170 ? 50.067 -28.927 8.908 1.00 43.85 ? 169 ILE A CB 1 ATOM 1275 C CG1 . ILE A 1 170 ? 51.167 -28.953 7.849 1.00 47.11 ? 169 ILE A CG1 1 ATOM 1276 C CG2 . ILE A 1 170 ? 50.611 -28.381 10.236 1.00 40.74 ? 169 ILE A CG2 1 ATOM 1277 C CD1 . ILE A 1 170 ? 51.708 -27.571 7.494 1.00 38.47 ? 169 ILE A CD1 1 ATOM 1278 N N . VAL A 1 171 ? 50.836 -32.224 8.538 1.00 47.37 ? 170 VAL A N 1 ATOM 1279 C CA . VAL A 1 171 ? 51.799 -33.293 8.766 1.00 45.45 ? 170 VAL A CA 1 ATOM 1280 C C . VAL A 1 171 ? 52.960 -33.071 7.817 1.00 55.02 ? 170 VAL A C 1 ATOM 1281 O O . VAL A 1 171 ? 52.759 -32.958 6.602 1.00 60.41 ? 170 VAL A O 1 ATOM 1282 C CB . VAL A 1 171 ? 51.177 -34.685 8.552 1.00 45.17 ? 170 VAL A CB 1 ATOM 1283 C CG1 . VAL A 1 171 ? 52.241 -35.761 8.643 1.00 46.69 ? 170 VAL A CG1 1 ATOM 1284 C CG2 . VAL A 1 171 ? 50.103 -34.940 9.576 1.00 50.81 ? 170 VAL A CG2 1 ATOM 1285 N N . SER A 1 172 ? 54.169 -32.995 8.367 1.00 52.67 ? 171 SER A N 1 ATOM 1286 C CA . SER A 1 172 ? 55.364 -32.704 7.585 1.00 54.65 ? 171 SER A CA 1 ATOM 1287 C C . SER A 1 172 ? 56.340 -33.857 7.740 1.00 52.68 ? 171 SER A C 1 ATOM 1288 O O . SER A 1 172 ? 56.756 -34.181 8.860 1.00 52.27 ? 171 SER A O 1 ATOM 1289 C CB . SER A 1 172 ? 56.009 -31.381 8.015 1.00 56.01 ? 171 SER A CB 1 ATOM 1290 O OG . SER A 1 172 ? 57.197 -31.120 7.278 1.00 55.22 ? 171 SER A OG 1 ATOM 1291 N N . GLN A 1 173 ? 56.677 -34.491 6.622 1.00 59.90 ? 172 GLN A N 1 ATOM 1292 C CA . GLN A 1 173 ? 57.715 -35.510 6.576 1.00 67.56 ? 172 GLN A CA 1 ATOM 1293 C C . GLN A 1 173 ? 59.004 -34.885 6.071 1.00 65.03 ? 172 GLN A C 1 ATOM 1294 O O . GLN A 1 173 ? 58.995 -34.152 5.073 1.00 59.26 ? 172 GLN A O 1 ATOM 1295 C CB . GLN A 1 173 ? 57.324 -36.671 5.668 1.00 62.70 ? 172 GLN A CB 1 ATOM 1296 C CG . GLN A 1 173 ? 56.132 -37.433 6.136 1.00 66.25 ? 172 GLN A CG 1 ATOM 1297 C CD . GLN A 1 173 ? 55.649 -38.397 5.084 1.00 74.01 ? 172 GLN A CD 1 ATOM 1298 O OE1 . GLN A 1 173 ? 56.132 -38.389 3.943 1.00 66.00 ? 172 GLN A OE1 1 ATOM 1299 N NE2 . GLN A 1 173 ? 54.691 -39.240 5.455 1.00 77.40 ? 172 GLN A NE2 1 ATOM 1300 N N . TYR A 1 174 ? 60.101 -35.174 6.767 1.00 65.74 ? 173 TYR A N 1 ATOM 1301 C CA . TYR A 1 174 ? 61.437 -34.749 6.370 1.00 57.20 ? 173 TYR A CA 1 ATOM 1302 C C . TYR A 1 174 ? 62.132 -35.927 5.703 1.00 60.61 ? 173 TYR A C 1 ATOM 1303 O O . TYR A 1 174 ? 62.339 -36.969 6.334 1.00 60.38 ? 173 TYR A O 1 ATOM 1304 C CB . TYR A 1 174 ? 62.238 -34.263 7.575 1.00 56.64 ? 173 TYR A CB 1 ATOM 1305 C CG . TYR A 1 174 ? 63.400 -33.376 7.212 1.00 65.56 ? 173 TYR A CG 1 ATOM 1306 C CD1 . TYR A 1 174 ? 63.179 -32.107 6.684 1.00 64.60 ? 173 TYR A CD1 1 ATOM 1307 C CD2 . TYR A 1 174 ? 64.717 -33.796 7.399 1.00 56.48 ? 173 TYR A CD2 1 ATOM 1308 C CE1 . TYR A 1 174 ? 64.228 -31.278 6.343 1.00 66.30 ? 173 TYR A CE1 1 ATOM 1309 C CE2 . TYR A 1 174 ? 65.777 -32.976 7.064 1.00 64.42 ? 173 TYR A CE2 1 ATOM 1310 C CZ . TYR A 1 174 ? 65.526 -31.715 6.537 1.00 73.08 ? 173 TYR A CZ 1 ATOM 1311 O OH . TYR A 1 174 ? 66.565 -30.878 6.199 1.00 69.35 ? 173 TYR A OH 1 ATOM 1312 N N A LYS A 1 175 ? 62.494 -35.759 4.437 0.27 66.41 ? 174 LYS A N 1 ATOM 1313 N N B LYS A 1 175 ? 62.471 -35.770 4.431 0.73 66.22 ? 174 LYS A N 1 ATOM 1314 C CA A LYS A 1 175 ? 63.133 -36.809 3.662 0.27 71.59 ? 174 LYS A CA 1 ATOM 1315 C CA B LYS A 1 175 ? 63.137 -36.818 3.675 0.73 71.74 ? 174 LYS A CA 1 ATOM 1316 C C A LYS A 1 175 ? 64.590 -36.454 3.386 0.27 73.66 ? 174 LYS A C 1 ATOM 1317 C C B LYS A 1 175 ? 64.598 -36.453 3.433 0.73 73.62 ? 174 LYS A C 1 ATOM 1318 O O A LYS A 1 175 ? 64.941 -35.283 3.205 0.27 71.63 ? 174 LYS A O 1 ATOM 1319 O O B LYS A 1 175 ? 64.957 -35.275 3.326 0.73 71.70 ? 174 LYS A O 1 ATOM 1320 C CB A LYS A 1 175 ? 62.388 -37.043 2.346 0.27 71.42 ? 174 LYS A CB 1 ATOM 1321 C CB B LYS A 1 175 ? 62.426 -37.074 2.342 0.73 71.56 ? 174 LYS A CB 1 ATOM 1322 C CG A LYS A 1 175 ? 60.943 -37.479 2.541 0.27 71.24 ? 174 LYS A CG 1 ATOM 1323 C CG B LYS A 1 175 ? 60.979 -37.519 2.511 0.73 71.19 ? 174 LYS A CG 1 ATOM 1324 C CD A LYS A 1 175 ? 60.183 -37.488 1.228 0.27 73.24 ? 174 LYS A CD 1 ATOM 1325 C CD B LYS A 1 175 ? 60.018 -36.569 1.811 0.73 72.35 ? 174 LYS A CD 1 ATOM 1326 C CE A LYS A 1 175 ? 60.087 -36.091 0.640 0.27 73.42 ? 174 LYS A CE 1 ATOM 1327 C CE B LYS A 1 175 ? 60.304 -36.517 0.325 0.73 73.60 ? 174 LYS A CE 1 ATOM 1328 N NZ A LYS A 1 175 ? 59.480 -36.113 -0.715 0.27 74.21 ? 174 LYS A NZ 1 ATOM 1329 N NZ B LYS A 1 175 ? 59.584 -35.410 -0.337 0.73 72.51 ? 174 LYS A NZ 1 ATOM 1330 N N . LEU A 1 176 ? 65.438 -37.482 3.359 1.00 76.05 ? 175 LEU A N 1 ATOM 1331 C CA . LEU A 1 176 ? 66.866 -37.295 3.158 1.00 74.00 ? 175 LEU A CA 1 ATOM 1332 C C . LEU A 1 176 ? 67.462 -38.544 2.531 1.00 79.97 ? 175 LEU A C 1 ATOM 1333 O O . LEU A 1 176 ? 66.914 -39.638 2.641 1.00 85.66 ? 175 LEU A O 1 ATOM 1334 C CB . LEU A 1 176 ? 67.580 -36.994 4.479 1.00 82.39 ? 175 LEU A CB 1 ATOM 1335 C CG . LEU A 1 176 ? 67.369 -37.905 5.699 1.00 84.88 ? 175 LEU A CG 1 ATOM 1336 C CD1 . LEU A 1 176 ? 68.158 -39.208 5.645 1.00 77.79 ? 175 LEU A CD1 1 ATOM 1337 C CD2 . LEU A 1 176 ? 67.719 -37.138 6.963 1.00 80.00 ? 175 LEU A CD2 1 ATOM 1338 N N . PHE A 1 177 ? 68.631 -38.373 1.909 1.00 91.34 ? 176 PHE A N 1 ATOM 1339 C CA . PHE A 1 177 ? 69.437 -39.507 1.479 1.00 92.49 ? 176 PHE A CA 1 ATOM 1340 C C . PHE A 1 177 ? 70.433 -39.818 2.577 1.00 93.38 ? 176 PHE A C 1 ATOM 1341 O O . PHE A 1 177 ? 71.385 -39.028 2.788 1.00 92.47 ? 176 PHE A O 1 ATOM 1342 C CB . PHE A 1 177 ? 70.154 -39.220 0.182 1.00 83.79 ? 176 PHE A CB 1 ATOM 1343 C CG . PHE A 1 177 ? 69.288 -38.636 -0.884 1.00 87.35 ? 176 PHE A CG 1 ATOM 1344 C CD1 . PHE A 1 177 ? 69.099 -37.270 -0.983 1.00 95.74 ? 176 PHE A CD1 1 ATOM 1345 C CD2 . PHE A 1 177 ? 68.653 -39.459 -1.793 1.00 91.41 ? 176 PHE A CD2 1 ATOM 1346 C CE1 . PHE A 1 177 ? 68.306 -36.737 -1.965 1.00 96.32 ? 176 PHE A CE1 1 ATOM 1347 C CE2 . PHE A 1 177 ? 67.850 -38.934 -2.778 1.00 96.76 ? 176 PHE A CE2 1 ATOM 1348 C CZ . PHE A 1 177 ? 67.676 -37.568 -2.867 1.00 92.39 ? 176 PHE A CZ 1 ATOM 1349 N N . PRO A 1 178 ? 70.294 -40.951 3.271 1.00 95.74 ? 177 PRO A N 1 ATOM 1350 C CA . PRO A 1 178 ? 71.163 -41.193 4.441 1.00 96.16 ? 177 PRO A CA 1 ATOM 1351 C C . PRO A 1 178 ? 72.639 -41.318 4.066 1.00 102.66 ? 177 PRO A C 1 ATOM 1352 O O . PRO A 1 178 ? 72.980 -41.795 2.982 1.00 96.32 ? 177 PRO A O 1 ATOM 1353 C CB . PRO A 1 178 ? 70.620 -42.498 5.053 1.00 91.37 ? 177 PRO A CB 1 ATOM 1354 C CG . PRO A 1 178 ? 69.482 -42.926 4.161 1.00 98.46 ? 177 PRO A CG 1 ATOM 1355 C CD . PRO A 1 178 ? 69.521 -42.149 2.899 1.00 96.93 ? 177 PRO A CD 1 ATOM 1356 N N . THR A 1 179 ? 73.496 -40.813 4.953 1.00 106.40 ? 178 THR A N 1 ATOM 1357 C CA . THR A 1 179 ? 74.944 -40.811 4.775 1.00 108.63 ? 178 THR A CA 1 ATOM 1358 C C . THR A 1 179 ? 75.629 -41.023 6.121 1.00 110.30 ? 178 THR A C 1 ATOM 1359 O O . THR A 1 179 ? 75.126 -40.579 7.157 1.00 109.68 ? 178 THR A O 1 ATOM 1360 C CB . THR A 1 179 ? 75.451 -39.505 4.148 1.00 108.68 ? 178 THR A CB 1 ATOM 1361 O OG1 . THR A 1 179 ? 74.505 -39.024 3.180 1.00 108.00 ? 178 THR A OG1 1 ATOM 1362 C CG2 . THR A 1 179 ? 76.793 -39.731 3.462 1.00 108.47 ? 178 THR A CG2 1 ATOM 1363 N N . ARG A 1 180 ? 76.767 -41.732 6.093 1.00 114.83 ? 179 ARG A N 1 ATOM 1364 C CA . ARG A 1 180 ? 77.652 -41.768 7.254 1.00 113.26 ? 179 ARG A CA 1 ATOM 1365 C C . ARG A 1 180 ? 77.962 -40.365 7.752 1.00 113.06 ? 179 ARG A C 1 ATOM 1366 O O . ARG A 1 180 ? 78.179 -40.158 8.954 1.00 110.67 ? 179 ARG A O 1 ATOM 1367 C CB . ARG A 1 180 ? 78.971 -42.482 6.917 1.00 114.43 ? 179 ARG A CB 1 ATOM 1368 C CG . ARG A 1 180 ? 78.848 -43.961 6.646 1.00 105.88 ? 179 ARG A CG 1 ATOM 1369 C CD . ARG A 1 180 ? 78.529 -44.718 7.911 1.00 97.90 ? 179 ARG A CD 1 ATOM 1370 N NE . ARG A 1 180 ? 78.352 -46.135 7.630 1.00 100.33 ? 179 ARG A NE 1 ATOM 1371 C CZ . ARG A 1 180 ? 77.199 -46.671 7.240 1.00 113.16 ? 179 ARG A CZ 1 ATOM 1372 N NH1 . ARG A 1 180 ? 77.116 -47.976 7.005 1.00 114.71 ? 179 ARG A NH1 1 ATOM 1373 N NH2 . ARG A 1 180 ? 76.124 -45.901 7.083 1.00 110.46 ? 179 ARG A NH2 1 ATOM 1374 N N . PHE A 1 181 ? 77.995 -39.395 6.836 1.00 114.58 ? 180 PHE A N 1 ATOM 1375 C CA . PHE A 1 181 ? 78.210 -37.995 7.169 1.00 112.86 ? 180 PHE A CA 1 ATOM 1376 C C . PHE A 1 181 ? 77.108 -37.432 8.063 1.00 111.64 ? 180 PHE A C 1 ATOM 1377 O O . PHE A 1 181 ? 77.363 -36.486 8.816 1.00 109.30 ? 180 PHE A O 1 ATOM 1378 C CB . PHE A 1 181 ? 78.338 -37.201 5.858 1.00 115.10 ? 180 PHE A CB 1 ATOM 1379 C CG . PHE A 1 181 ? 78.317 -35.704 6.024 1.00 120.78 ? 180 PHE A CG 1 ATOM 1380 C CD1 . PHE A 1 181 ? 79.429 -35.029 6.518 1.00 124.89 ? 180 PHE A CD1 1 ATOM 1381 C CD2 . PHE A 1 181 ? 77.206 -34.968 5.642 1.00 113.62 ? 180 PHE A CD2 1 ATOM 1382 C CE1 . PHE A 1 181 ? 79.420 -33.651 6.660 1.00 114.55 ? 180 PHE A CE1 1 ATOM 1383 C CE2 . PHE A 1 181 ? 77.191 -33.591 5.778 1.00 116.69 ? 180 PHE A CE2 1 ATOM 1384 C CZ . PHE A 1 181 ? 78.302 -32.932 6.285 1.00 114.33 ? 180 PHE A CZ 1 ATOM 1385 N N . ALA A 1 182 ? 75.903 -38.007 8.027 1.00 105.33 ? 181 ALA A N 1 ATOM 1386 C CA . ALA A 1 182 ? 74.773 -37.446 8.754 1.00 101.65 ? 181 ALA A CA 1 ATOM 1387 C C . ALA A 1 182 ? 74.602 -38.004 10.164 1.00 96.96 ? 181 ALA A C 1 ATOM 1388 O O . ALA A 1 182 ? 73.755 -37.499 10.905 1.00 90.22 ? 181 ALA A O 1 ATOM 1389 C CB . ALA A 1 182 ? 73.472 -37.663 7.971 1.00 91.67 ? 181 ALA A CB 1 ATOM 1390 N N . ARG A 1 183 ? 75.354 -39.026 10.566 1.00 91.14 ? 182 ARG A N 1 ATOM 1391 C CA . ARG A 1 183 ? 75.160 -39.539 11.915 1.00 95.73 ? 182 ARG A CA 1 ATOM 1392 C C . ARG A 1 183 ? 75.848 -38.629 12.922 1.00 91.45 ? 182 ARG A C 1 ATOM 1393 O O . ARG A 1 183 ? 76.826 -37.944 12.611 1.00 89.58 ? 182 ARG A O 1 ATOM 1394 C CB . ARG A 1 183 ? 75.673 -40.972 12.063 1.00 99.53 ? 182 ARG A CB 1 ATOM 1395 C CG . ARG A 1 183 ? 76.995 -41.124 12.781 1.00 99.26 ? 182 ARG A CG 1 ATOM 1396 C CD . ARG A 1 183 ? 77.234 -42.580 13.161 1.00 97.50 ? 182 ARG A CD 1 ATOM 1397 N NE . ARG A 1 183 ? 77.441 -43.443 12.000 1.00 96.21 ? 182 ARG A NE 1 ATOM 1398 C CZ . ARG A 1 183 ? 77.594 -44.761 12.076 1.00 81.53 ? 182 ARG A CZ 1 ATOM 1399 N NH1 . ARG A 1 183 ? 77.570 -45.360 13.255 1.00 80.51 ? 182 ARG A NH1 1 ATOM 1400 N NH2 . ARG A 1 183 ? 77.775 -45.478 10.981 1.00 87.43 ? 182 ARG A NH2 1 ATOM 1401 N N . GLY A 1 184 ? 75.321 -38.632 14.143 1.00 93.59 ? 183 GLY A N 1 ATOM 1402 C CA . GLY A 1 184 ? 75.618 -37.598 15.100 1.00 84.42 ? 183 GLY A CA 1 ATOM 1403 C C . GLY A 1 184 ? 74.865 -36.304 14.870 1.00 79.19 ? 183 GLY A C 1 ATOM 1404 O O . GLY A 1 184 ? 74.720 -35.524 15.815 1.00 73.74 ? 183 GLY A O 1 ATOM 1405 N N . ARG A 1 185 ? 74.385 -36.047 13.644 1.00 79.35 ? 184 ARG A N 1 ATOM 1406 C CA . ARG A 1 185 ? 73.564 -34.866 13.375 1.00 77.77 ? 184 ARG A CA 1 ATOM 1407 C C . ARG A 1 185 ? 72.245 -34.906 14.122 1.00 72.75 ? 184 ARG A C 1 ATOM 1408 O O . ARG A 1 185 ? 71.656 -35.966 14.343 1.00 72.60 ? 184 ARG A O 1 ATOM 1409 C CB . ARG A 1 185 ? 73.218 -34.684 11.887 1.00 84.40 ? 184 ARG A CB 1 ATOM 1410 C CG . ARG A 1 185 ? 74.388 -34.480 10.941 1.00 86.45 ? 184 ARG A CG 1 ATOM 1411 C CD . ARG A 1 185 ? 75.342 -33.359 11.390 1.00 86.46 ? 184 ARG A CD 1 ATOM 1412 N NE . ARG A 1 185 ? 76.367 -33.912 12.268 1.00 96.32 ? 184 ARG A NE 1 ATOM 1413 C CZ . ARG A 1 185 ? 77.614 -34.147 11.871 1.00 98.36 ? 184 ARG A CZ 1 ATOM 1414 N NH1 . ARG A 1 185 ? 78.005 -33.882 10.626 1.00 105.13 ? 184 ARG A NH1 1 ATOM 1415 N NH2 . ARG A 1 185 ? 78.493 -34.655 12.713 1.00 87.24 ? 184 ARG A NH2 1 ATOM 1416 N N . ARG A 1 186 ? 71.753 -33.717 14.456 1.00 68.16 ? 185 ARG A N 1 ATOM 1417 C CA . ARG A 1 186 ? 70.432 -33.547 15.042 1.00 69.94 ? 185 ARG A CA 1 ATOM 1418 C C . ARG A 1 186 ? 69.513 -32.852 14.044 1.00 64.26 ? 185 ARG A C 1 ATOM 1419 O O . ARG A 1 186 ? 69.882 -31.826 13.465 1.00 64.34 ? 185 ARG A O 1 ATOM 1420 C CB . ARG A 1 186 ? 70.514 -32.742 16.338 1.00 63.83 ? 185 ARG A CB 1 ATOM 1421 C CG . ARG A 1 186 ? 69.183 -32.427 16.940 1.00 57.41 ? 185 ARG A CG 1 ATOM 1422 C CD . ARG A 1 186 ? 69.350 -31.532 18.134 1.00 52.85 ? 185 ARG A CD 1 ATOM 1423 N NE . ARG A 1 186 ? 70.191 -32.130 19.158 1.00 53.66 ? 185 ARG A NE 1 ATOM 1424 C CZ . ARG A 1 186 ? 69.754 -32.992 20.069 1.00 61.07 ? 185 ARG A CZ 1 ATOM 1425 N NH1 . ARG A 1 186 ? 70.588 -33.483 20.981 1.00 56.43 ? 185 ARG A NH1 1 ATOM 1426 N NH2 . ARG A 1 186 ? 68.482 -33.368 20.066 1.00 54.79 ? 185 ARG A NH2 1 ATOM 1427 N N . ILE A 1 187 ? 68.332 -33.430 13.823 1.00 60.39 ? 186 ILE A N 1 ATOM 1428 C CA . ILE A 1 187 ? 67.276 -32.791 13.039 1.00 64.39 ? 186 ILE A CA 1 ATOM 1429 C C . ILE A 1 187 ? 66.279 -32.179 14.004 1.00 56.40 ? 186 ILE A C 1 ATOM 1430 O O . ILE A 1 187 ? 65.988 -32.758 15.056 1.00 57.20 ? 186 ILE A O 1 ATOM 1431 C CB . ILE A 1 187 ? 66.564 -33.782 12.097 1.00 68.87 ? 186 ILE A CB 1 ATOM 1432 C CG1 . ILE A 1 187 ? 66.291 -35.101 12.809 1.00 63.44 ? 186 ILE A CG1 1 ATOM 1433 C CG2 . ILE A 1 187 ? 67.362 -34.011 10.832 1.00 75.82 ? 186 ILE A CG2 1 ATOM 1434 C CD1 . ILE A 1 187 ? 65.410 -35.979 12.017 1.00 69.63 ? 186 ILE A CD1 1 ATOM 1435 N N . THR A 1 188 ? 65.730 -31.027 13.636 1.00 54.54 ? 187 THR A N 1 ATOM 1436 C CA . THR A 1 188 ? 64.862 -30.268 14.525 1.00 53.41 ? 187 THR A CA 1 ATOM 1437 C C . THR A 1 188 ? 63.592 -29.871 13.788 1.00 48.60 ? 187 THR A C 1 ATOM 1438 O O . THR A 1 188 ? 63.655 -29.381 12.657 1.00 46.45 ? 187 THR A O 1 ATOM 1439 C CB . THR A 1 188 ? 65.596 -29.028 15.071 1.00 47.60 ? 187 THR A CB 1 ATOM 1440 O OG1 . THR A 1 188 ? 66.766 -29.453 15.785 1.00 55.93 ? 187 THR A OG1 1 ATOM 1441 C CG2 . THR A 1 188 ? 64.705 -28.239 16.017 1.00 40.76 ? 187 THR A CG2 1 ATOM 1442 N N . CYS A 1 189 ? 62.444 -30.108 14.423 1.00 51.08 ? 188 CYS A N 1 ATOM 1443 C CA . CYS A 1 189 ? 61.159 -29.608 13.948 1.00 53.37 ? 188 CYS A CA 1 ATOM 1444 C C . CYS A 1 189 ? 60.835 -28.307 14.679 1.00 43.88 ? 188 CYS A C 1 ATOM 1445 O O . CYS A 1 189 ? 60.925 -28.239 15.911 1.00 43.61 ? 188 CYS A O 1 ATOM 1446 C CB . CYS A 1 189 ? 60.023 -30.620 14.164 1.00 42.77 ? 188 CYS A CB 1 ATOM 1447 S SG . CYS A 1 189 ? 58.460 -29.915 13.573 1.00 73.71 ? 188 CYS A SG 1 ATOM 1448 N N . VAL A 1 190 ? 60.447 -27.288 13.920 1.00 38.70 ? 189 VAL A N 1 ATOM 1449 C CA . VAL A 1 190 ? 60.051 -25.993 14.457 1.00 35.55 ? 189 VAL A CA 1 ATOM 1450 C C . VAL A 1 190 ? 58.636 -25.744 13.981 1.00 38.84 ? 189 VAL A C 1 ATOM 1451 O O . VAL A 1 190 ? 58.378 -25.760 12.773 1.00 42.44 ? 189 VAL A O 1 ATOM 1452 C CB . VAL A 1 190 ? 60.987 -24.863 13.986 1.00 38.32 ? 189 VAL A CB 1 ATOM 1453 C CG1 . VAL A 1 190 ? 60.510 -23.481 14.486 1.00 29.48 ? 189 VAL A CG1 1 ATOM 1454 C CG2 . VAL A 1 190 ? 62.426 -25.131 14.417 1.00 42.72 ? 189 VAL A CG2 1 ATOM 1455 N N A VAL A 1 191 ? 57.739 -25.451 14.921 0.87 36.57 ? 190 VAL A N 1 ATOM 1456 N N B VAL A 1 191 ? 57.708 -25.572 14.914 0.13 36.52 ? 190 VAL A N 1 ATOM 1457 C CA A VAL A 1 191 ? 56.315 -25.254 14.655 0.87 35.41 ? 190 VAL A CA 1 ATOM 1458 C CA B VAL A 1 191 ? 56.332 -25.244 14.566 0.13 35.96 ? 190 VAL A CA 1 ATOM 1459 C C A VAL A 1 191 ? 55.921 -23.846 15.085 0.87 31.87 ? 190 VAL A C 1 ATOM 1460 C C B VAL A 1 191 ? 56.054 -23.818 15.016 0.13 32.37 ? 190 VAL A C 1 ATOM 1461 O O A VAL A 1 191 ? 56.061 -23.489 16.259 0.87 30.87 ? 190 VAL A O 1 ATOM 1462 O O B VAL A 1 191 ? 56.481 -23.394 16.097 0.13 33.07 ? 190 VAL A O 1 ATOM 1463 C CB A VAL A 1 191 ? 55.460 -26.304 15.387 0.87 35.96 ? 190 VAL A CB 1 ATOM 1464 C CB B VAL A 1 191 ? 55.314 -26.249 15.152 0.13 35.61 ? 190 VAL A CB 1 ATOM 1465 C CG1 A VAL A 1 191 ? 53.982 -26.021 15.200 0.87 36.76 ? 190 VAL A CG1 1 ATOM 1466 C CG1 B VAL A 1 191 ? 55.935 -27.640 15.259 0.13 36.56 ? 190 VAL A CG1 1 ATOM 1467 C CG2 A VAL A 1 191 ? 55.819 -27.728 14.914 0.87 36.70 ? 190 VAL A CG2 1 ATOM 1468 C CG2 B VAL A 1 191 ? 54.745 -25.787 16.489 0.13 34.49 ? 190 VAL A CG2 1 ATOM 1469 N N . LYS A 1 192 ? 55.389 -23.064 14.151 1.00 29.64 ? 191 LYS A N 1 ATOM 1470 C CA . LYS A 1 192 ? 54.977 -21.690 14.421 1.00 34.34 ? 191 LYS A CA 1 ATOM 1471 C C . LYS A 1 192 ? 53.453 -21.589 14.472 1.00 37.37 ? 191 LYS A C 1 ATOM 1472 O O . LYS A 1 192 ? 52.752 -22.159 13.634 1.00 32.20 ? 191 LYS A O 1 ATOM 1473 C CB . LYS A 1 192 ? 55.520 -20.741 13.355 1.00 26.86 ? 191 LYS A CB 1 ATOM 1474 C CG . LYS A 1 192 ? 56.989 -20.829 13.211 1.00 36.05 ? 191 LYS A CG 1 ATOM 1475 C CD . LYS A 1 192 ? 57.442 -20.228 11.916 1.00 32.03 ? 191 LYS A CD 1 ATOM 1476 C CE . LYS A 1 192 ? 58.934 -20.454 11.761 1.00 34.99 ? 191 LYS A CE 1 ATOM 1477 N NZ . LYS A 1 192 ? 59.695 -19.669 12.770 1.00 37.73 ? 191 LYS A NZ 1 ATOM 1478 N N . HIS A 1 193 ? 52.939 -20.854 15.454 1.00 34.65 ? 192 HIS A N 1 ATOM 1479 C CA . HIS A 1 193 ? 51.504 -20.722 15.564 1.00 30.65 ? 192 HIS A CA 1 ATOM 1480 C C . HIS A 1 193 ? 51.181 -19.524 16.435 1.00 31.73 ? 192 HIS A C 1 ATOM 1481 O O . HIS A 1 193 ? 51.823 -19.347 17.479 1.00 33.64 ? 192 HIS A O 1 ATOM 1482 C CB . HIS A 1 193 ? 50.858 -21.986 16.147 1.00 33.63 ? 192 HIS A CB 1 ATOM 1483 C CG . HIS A 1 193 ? 49.353 -21.946 16.140 1.00 35.68 ? 192 HIS A CG 1 ATOM 1484 N ND1 . HIS A 1 193 ? 48.610 -21.504 17.215 1.00 34.84 ? 192 HIS A ND1 1 ATOM 1485 C CD2 . HIS A 1 193 ? 48.457 -22.274 15.180 1.00 34.60 ? 192 HIS A CD2 1 ATOM 1486 C CE1 . HIS A 1 193 ? 47.325 -21.572 16.921 1.00 32.32 ? 192 HIS A CE1 1 ATOM 1487 N NE2 . HIS A 1 193 ? 47.204 -22.035 15.691 1.00 33.96 ? 192 HIS A NE2 1 ATOM 1488 N N . PRO A 1 194 ? 50.178 -18.716 16.071 1.00 31.78 ? 193 PRO A N 1 ATOM 1489 C CA . PRO A 1 194 ? 49.861 -17.521 16.866 1.00 33.06 ? 193 PRO A CA 1 ATOM 1490 C C . PRO A 1 194 ? 49.411 -17.800 18.293 1.00 33.96 ? 193 PRO A C 1 ATOM 1491 O O . PRO A 1 194 ? 49.459 -16.879 19.118 1.00 31.08 ? 193 PRO A O 1 ATOM 1492 C CB . PRO A 1 194 ? 48.751 -16.840 16.050 1.00 24.94 ? 193 PRO A CB 1 ATOM 1493 C CG . PRO A 1 194 ? 48.227 -17.855 15.169 1.00 27.13 ? 193 PRO A CG 1 ATOM 1494 C CD . PRO A 1 194 ? 49.376 -18.766 14.843 1.00 31.08 ? 193 PRO A CD 1 ATOM 1495 N N . ALA A 1 195 ? 48.984 -19.019 18.631 1.00 32.42 ? 194 ALA A N 1 ATOM 1496 C CA . ALA A 1 195 ? 48.623 -19.271 20.021 1.00 28.28 ? 194 ALA A CA 1 ATOM 1497 C C . ALA A 1 195 ? 49.841 -19.533 20.885 1.00 37.27 ? 194 ALA A C 1 ATOM 1498 O O . ALA A 1 195 ? 49.705 -19.627 22.113 1.00 37.61 ? 194 ALA A O 1 ATOM 1499 C CB . ALA A 1 195 ? 47.660 -20.452 20.125 1.00 28.35 ? 194 ALA A CB 1 ATOM 1500 N N . LEU A 1 196 ? 51.017 -19.646 20.267 1.00 33.20 ? 195 LEU A N 1 ATOM 1501 C CA . LEU A 1 196 ? 52.260 -19.966 20.954 1.00 35.43 ? 195 LEU A CA 1 ATOM 1502 C C . LEU A 1 196 ? 53.049 -18.690 21.258 1.00 43.41 ? 195 LEU A C 1 ATOM 1503 O O . LEU A 1 196 ? 53.166 -17.797 20.403 1.00 37.54 ? 195 LEU A O 1 ATOM 1504 C CB . LEU A 1 196 ? 53.098 -20.935 20.115 1.00 32.68 ? 195 LEU A CB 1 ATOM 1505 C CG . LEU A 1 196 ? 52.386 -22.247 19.771 1.00 37.61 ? 195 LEU A CG 1 ATOM 1506 C CD1 . LEU A 1 196 ? 53.176 -23.078 18.791 1.00 32.43 ? 195 LEU A CD1 1 ATOM 1507 C CD2 . LEU A 1 196 ? 52.103 -23.055 21.026 1.00 37.44 ? 195 LEU A CD2 1 ATOM 1508 N N . GLU A 1 197 ? 53.554 -18.605 22.500 1.00 40.58 ? 196 GLU A N 1 ATOM 1509 C CA . GLU A 1 197 ? 54.451 -17.519 22.894 1.00 46.20 ? 196 GLU A CA 1 ATOM 1510 C C . GLU A 1 197 ? 55.785 -17.607 22.153 1.00 42.39 ? 196 GLU A C 1 ATOM 1511 O O . GLU A 1 197 ? 56.342 -16.583 21.744 1.00 41.76 ? 196 GLU A O 1 ATOM 1512 C CB . GLU A 1 197 ? 54.674 -17.557 24.412 1.00 50.91 ? 196 GLU A CB 1 ATOM 1513 C CG . GLU A 1 197 ? 55.157 -16.235 25.030 1.00 68.09 ? 196 GLU A CG 1 ATOM 1514 C CD . GLU A 1 197 ? 56.374 -16.386 25.929 1.00 73.26 ? 196 GLU A CD 1 ATOM 1515 O OE1 . GLU A 1 197 ? 56.910 -17.500 26.085 1.00 70.65 ? 196 GLU A OE1 1 ATOM 1516 O OE2 . GLU A 1 197 ? 56.801 -15.375 26.506 1.00 62.36 ? 196 GLU A OE2 1 ATOM 1517 N N . LYS A 1 198 ? 56.306 -18.818 21.974 1.00 33.59 ? 197 LYS A N 1 ATOM 1518 C CA . LYS A 1 198 ? 57.468 -19.103 21.157 1.00 33.48 ? 197 LYS A CA 1 ATOM 1519 C C . LYS A 1 198 ? 57.153 -20.276 20.250 1.00 29.02 ? 197 LYS A C 1 ATOM 1520 O O . LYS A 1 198 ? 56.199 -21.009 20.483 1.00 32.33 ? 197 LYS A O 1 ATOM 1521 C CB . LYS A 1 198 ? 58.688 -19.447 22.018 1.00 41.18 ? 197 LYS A CB 1 ATOM 1522 C CG . LYS A 1 198 ? 59.290 -18.222 22.621 1.00 52.30 ? 197 LYS A CG 1 ATOM 1523 C CD . LYS A 1 198 ? 59.524 -18.408 24.105 1.00 57.92 ? 197 LYS A CD 1 ATOM 1524 C CE . LYS A 1 198 ? 60.652 -17.525 24.588 1.00 57.20 ? 197 LYS A CE 1 ATOM 1525 N NZ . LYS A 1 198 ? 61.133 -17.880 25.953 1.00 56.08 ? 197 LYS A NZ 1 ATOM 1526 N N . ASP A 1 199 ? 57.985 -20.467 19.227 1.00 30.94 ? 198 ASP A N 1 ATOM 1527 C CA . ASP A 1 199 ? 57.913 -21.679 18.421 1.00 30.90 ? 198 ASP A CA 1 ATOM 1528 C C . ASP A 1 199 ? 58.201 -22.922 19.263 1.00 37.53 ? 198 ASP A C 1 ATOM 1529 O O . ASP A 1 199 ? 59.099 -22.937 20.111 1.00 36.40 ? 198 ASP A O 1 ATOM 1530 C CB . ASP A 1 199 ? 58.912 -21.607 17.268 1.00 37.47 ? 198 ASP A CB 1 ATOM 1531 C CG . ASP A 1 199 ? 58.685 -20.408 16.370 1.00 39.65 ? 198 ASP A CG 1 ATOM 1532 O OD1 . ASP A 1 199 ? 57.612 -19.791 16.488 1.00 37.34 ? 198 ASP A OD1 1 ATOM 1533 O OD2 . ASP A 1 199 ? 59.579 -20.090 15.548 1.00 38.65 ? 198 ASP A OD2 1 ATOM 1534 N N . ILE A 1 200 ? 57.433 -23.975 19.024 1.00 38.51 ? 199 ILE A N 1 ATOM 1535 C CA . ILE A 1 200 ? 57.712 -25.271 19.632 1.00 37.96 ? 199 ILE A CA 1 ATOM 1536 C C . ILE A 1 200 ? 58.847 -25.924 18.859 1.00 41.30 ? 199 ILE A C 1 ATOM 1537 O O . ILE A 1 200 ? 58.931 -25.789 17.632 1.00 38.27 ? 199 ILE A O 1 ATOM 1538 C CB . ILE A 1 200 ? 56.445 -26.143 19.632 1.00 34.03 ? 199 ILE A CB 1 ATOM 1539 C CG1 . ILE A 1 200 ? 55.391 -25.524 20.543 1.00 36.66 ? 199 ILE A CG1 1 ATOM 1540 C CG2 . ILE A 1 200 ? 56.740 -27.564 20.054 1.00 35.56 ? 199 ILE A CG2 1 ATOM 1541 C CD1 . ILE A 1 200 ? 54.033 -26.177 20.427 1.00 27.03 ? 199 ILE A CD1 1 ATOM 1542 N N . ARG A 1 201 ? 59.736 -26.621 19.572 1.00 37.72 ? 200 ARG A N 1 ATOM 1543 C CA . ARG A 1 201 ? 60.885 -27.277 18.958 1.00 40.17 ? 200 ARG A CA 1 ATOM 1544 C C . ARG A 1 201 ? 61.061 -28.693 19.499 1.00 42.17 ? 200 ARG A C 1 ATOM 1545 O O . ARG A 1 201 ? 61.160 -28.897 20.714 1.00 43.96 ? 200 ARG A O 1 ATOM 1546 C CB . ARG A 1 201 ? 62.143 -26.442 19.184 1.00 39.28 ? 200 ARG A CB 1 ATOM 1547 C CG . ARG A 1 201 ? 62.113 -25.122 18.428 1.00 37.27 ? 200 ARG A CG 1 ATOM 1548 C CD . ARG A 1 201 ? 63.232 -24.177 18.867 1.00 39.51 ? 200 ARG A CD 1 ATOM 1549 N NE . ARG A 1 201 ? 63.457 -23.163 17.845 1.00 34.74 ? 200 ARG A NE 1 ATOM 1550 C CZ . ARG A 1 201 ? 64.330 -23.292 16.857 1.00 42.04 ? 200 ARG A CZ 1 ATOM 1551 N NH1 . ARG A 1 201 ? 65.086 -24.383 16.776 1.00 41.66 ? 200 ARG A NH1 1 ATOM 1552 N NH2 . ARG A 1 201 ? 64.441 -22.333 15.950 1.00 41.18 ? 200 ARG A NH2 1 ATOM 1553 N N . TYR A 1 202 ? 61.094 -29.672 18.603 1.00 36.19 ? 201 TYR A N 1 ATOM 1554 C CA . TYR A 1 202 ? 61.436 -31.041 18.971 1.00 46.63 ? 201 TYR A CA 1 ATOM 1555 C C . TYR A 1 202 ? 62.513 -31.518 18.012 1.00 48.18 ? 201 TYR A C 1 ATOM 1556 O O . TYR A 1 202 ? 62.417 -31.303 16.799 1.00 47.63 ? 201 TYR A O 1 ATOM 1557 C CB . TYR A 1 202 ? 60.226 -32.024 18.938 1.00 41.57 ? 201 TYR A CB 1 ATOM 1558 C CG . TYR A 1 202 ? 59.148 -31.690 19.932 1.00 42.11 ? 201 TYR A CG 1 ATOM 1559 C CD1 . TYR A 1 202 ? 59.405 -31.720 21.291 1.00 47.73 ? 201 TYR A CD1 1 ATOM 1560 C CD2 . TYR A 1 202 ? 57.862 -31.336 19.509 1.00 44.58 ? 201 TYR A CD2 1 ATOM 1561 C CE1 . TYR A 1 202 ? 58.418 -31.396 22.219 1.00 53.78 ? 201 TYR A CE1 1 ATOM 1562 C CE2 . TYR A 1 202 ? 56.863 -31.020 20.427 1.00 42.32 ? 201 TYR A CE2 1 ATOM 1563 C CZ . TYR A 1 202 ? 57.150 -31.047 21.783 1.00 52.57 ? 201 TYR A CZ 1 ATOM 1564 O OH . TYR A 1 202 ? 56.183 -30.731 22.714 1.00 58.01 ? 201 TYR A OH 1 ATOM 1565 N N . SER A 1 203 ? 63.534 -32.162 18.567 1.00 44.48 ? 202 SER A N 1 ATOM 1566 C CA . SER A 1 203 ? 64.703 -32.574 17.815 1.00 47.49 ? 202 SER A CA 1 ATOM 1567 C C . SER A 1 203 ? 65.154 -33.943 18.290 1.00 45.49 ? 202 SER A C 1 ATOM 1568 O O . SER A 1 203 ? 64.814 -34.388 19.386 1.00 52.23 ? 202 SER A O 1 ATOM 1569 C CB . SER A 1 203 ? 65.842 -31.577 17.998 1.00 51.17 ? 202 SER A CB 1 ATOM 1570 O OG . SER A 1 203 ? 66.250 -31.571 19.362 1.00 57.49 ? 202 SER A OG 1 ATOM 1571 N N . PHE A 1 204 ? 65.944 -34.605 17.458 1.00 52.37 ? 203 PHE A N 1 ATOM 1572 C CA . PHE A 1 204 ? 66.616 -35.822 17.889 1.00 60.40 ? 203 PHE A CA 1 ATOM 1573 C C . PHE A 1 204 ? 67.793 -36.089 16.961 1.00 65.40 ? 203 PHE A C 1 ATOM 1574 O O . PHE A 1 204 ? 67.834 -35.617 15.819 1.00 65.76 ? 203 PHE A O 1 ATOM 1575 C CB . PHE A 1 204 ? 65.663 -37.025 17.941 1.00 64.24 ? 203 PHE A CB 1 ATOM 1576 C CG . PHE A 1 204 ? 65.116 -37.441 16.603 1.00 61.16 ? 203 PHE A CG 1 ATOM 1577 C CD1 . PHE A 1 204 ? 63.908 -36.954 16.153 1.00 55.82 ? 203 PHE A CD1 1 ATOM 1578 C CD2 . PHE A 1 204 ? 65.811 -38.333 15.804 1.00 64.11 ? 203 PHE A CD2 1 ATOM 1579 C CE1 . PHE A 1 204 ? 63.411 -37.346 14.924 1.00 64.22 ? 203 PHE A CE1 1 ATOM 1580 C CE2 . PHE A 1 204 ? 65.319 -38.733 14.580 1.00 62.75 ? 203 PHE A CE2 1 ATOM 1581 C CZ . PHE A 1 204 ? 64.120 -38.242 14.140 1.00 66.96 ? 203 PHE A CZ 1 ATOM 1582 N N . ILE A 1 205 ? 68.755 -36.846 17.479 1.00 66.44 ? 204 ILE A N 1 ATOM 1583 C CA . ILE A 1 205 ? 69.957 -37.171 16.724 1.00 71.08 ? 204 ILE A CA 1 ATOM 1584 C C . ILE A 1 205 ? 69.633 -38.259 15.710 1.00 69.20 ? 204 ILE A C 1 ATOM 1585 O O . ILE A 1 205 ? 69.092 -39.309 16.070 1.00 61.51 ? 204 ILE A O 1 ATOM 1586 C CB . ILE A 1 205 ? 71.086 -37.616 17.667 1.00 76.41 ? 204 ILE A CB 1 ATOM 1587 C CG1 . ILE A 1 205 ? 71.297 -36.575 18.773 1.00 74.45 ? 204 ILE A CG1 1 ATOM 1588 C CG2 . ILE A 1 205 ? 72.376 -37.862 16.880 1.00 72.18 ? 204 ILE A CG2 1 ATOM 1589 C CD1 . ILE A 1 205 ? 72.037 -35.320 18.314 1.00 64.10 ? 204 ILE A CD1 1 ATOM 1590 N N . LEU A 1 206 ? 69.962 -38.001 14.441 1.00 71.66 ? 205 LEU A N 1 ATOM 1591 C CA . LEU A 1 206 ? 69.868 -39.018 13.400 1.00 65.79 ? 205 LEU A CA 1 ATOM 1592 C C . LEU A 1 206 ? 70.763 -40.204 13.714 1.00 75.61 ? 205 LEU A C 1 ATOM 1593 O O . LEU A 1 206 ? 71.930 -40.051 14.083 1.00 78.55 ? 205 LEU A O 1 ATOM 1594 C CB . LEU A 1 206 ? 70.264 -38.438 12.047 1.00 66.51 ? 205 LEU A CB 1 ATOM 1595 C CG . LEU A 1 206 ? 69.208 -37.584 11.363 1.00 79.18 ? 205 LEU A CG 1 ATOM 1596 C CD1 . LEU A 1 206 ? 69.675 -37.233 9.975 1.00 73.13 ? 205 LEU A CD1 1 ATOM 1597 C CD2 . LEU A 1 206 ? 67.885 -38.336 11.315 1.00 76.02 ? 205 LEU A CD2 1 ATOM 1598 N N . ASP A 1 207 ? 70.216 -41.388 13.550 1.00 78.75 ? 206 ASP A N 1 ATOM 1599 C CA . ASP A 1 207 ? 70.968 -42.618 13.696 1.00 79.13 ? 206 ASP A CA 1 ATOM 1600 C C . ASP A 1 207 ? 71.011 -43.249 12.317 1.00 86.41 ? 206 ASP A C 1 ATOM 1601 O O . ASP A 1 207 ? 69.992 -43.745 11.832 1.00 86.38 ? 206 ASP A O 1 ATOM 1602 C CB . ASP A 1 207 ? 70.302 -43.537 14.712 1.00 74.91 ? 206 ASP A CB 1 ATOM 1603 C CG . ASP A 1 207 ? 71.209 -44.619 15.175 1.00 77.19 ? 206 ASP A CG 1 ATOM 1604 O OD1 . ASP A 1 207 ? 72.234 -44.819 14.500 1.00 83.21 ? 206 ASP A OD1 1 ATOM 1605 O OD2 . ASP A 1 207 ? 70.895 -45.273 16.193 1.00 77.10 ? 206 ASP A OD2 1 ATOM 1606 N N . ILE A 1 208 ? 72.167 -43.207 11.660 1.00 98.69 ? 207 ILE A N 1 ATOM 1607 C CA . ILE A 1 208 ? 72.345 -43.926 10.402 1.00 102.13 ? 207 ILE A CA 1 ATOM 1608 C C . ILE A 1 208 ? 73.254 -45.123 10.653 1.00 97.81 ? 207 ILE A C 1 ATOM 1609 O O . ILE A 1 208 ? 74.332 -44.992 11.251 1.00 98.88 ? 207 ILE A O 1 ATOM 1610 C CB . ILE A 1 208 ? 72.882 -43.045 9.257 1.00 95.95 ? 207 ILE A CB 1 ATOM 1611 C CG1 . ILE A 1 208 ? 72.953 -43.877 8.013 1.00 101.32 ? 207 ILE A CG1 1 ATOM 1612 C CG2 . ILE A 1 208 ? 74.204 -42.501 9.555 1.00 99.66 ? 207 ILE A CG2 1 ATOM 1613 C CD1 . ILE A 1 208 ? 73.616 -43.337 6.911 1.00 101.80 ? 207 ILE A CD1 1 ATOM 1614 N N . GLN A 1 209 ? 72.818 -46.282 10.168 1.00 95.92 ? 208 GLN A N 1 ATOM 1615 C CA . GLN A 1 209 ? 73.372 -47.575 10.524 1.00 90.83 ? 208 GLN A CA 1 ATOM 1616 C C . GLN A 1 209 ? 73.512 -47.702 12.036 1.00 90.91 ? 208 GLN A C 1 ATOM 1617 O O . GLN A 1 209 ? 72.790 -47.054 12.793 1.00 86.60 ? 208 GLN A O 1 ATOM 1618 C CB . GLN A 1 209 ? 74.717 -47.803 9.856 1.00 95.59 ? 208 GLN A CB 1 ATOM 1619 C CG . GLN A 1 209 ? 75.359 -49.077 10.353 1.00 96.32 ? 208 GLN A CG 1 ATOM 1620 C CD . GLN A 1 209 ? 76.739 -49.276 9.814 1.00 81.05 ? 208 GLN A CD 1 ATOM 1621 O OE1 . GLN A 1 209 ? 76.917 -49.860 8.746 1.00 82.63 ? 208 GLN A OE1 1 ATOM 1622 N NE2 . GLN A 1 209 ? 77.734 -48.786 10.548 1.00 71.23 ? 208 GLN A NE2 1 ATOM 1623 N N . PRO B 1 1 ? 7.523 -5.094 22.853 1.00 48.72 ? 0 PRO B N 1 ATOM 1624 C CA . PRO B 1 1 ? 7.678 -6.319 23.654 1.00 55.64 ? 0 PRO B CA 1 ATOM 1625 C C . PRO B 1 1 ? 6.585 -6.450 24.728 1.00 53.28 ? 0 PRO B C 1 ATOM 1626 O O . PRO B 1 1 ? 5.390 -6.563 24.436 1.00 39.03 ? 0 PRO B O 1 ATOM 1627 C CB . PRO B 1 1 ? 9.069 -6.141 24.296 1.00 48.61 ? 0 PRO B CB 1 ATOM 1628 C CG . PRO B 1 1 ? 9.807 -5.126 23.366 1.00 46.84 ? 0 PRO B CG 1 ATOM 1629 C CD . PRO B 1 1 ? 8.812 -4.627 22.321 1.00 36.03 ? 0 PRO B CD 1 ATOM 1630 N N . SER B 1 2 ? 7.014 -6.457 25.984 1.00 55.56 ? 1 SER B N 1 ATOM 1631 C CA . SER B 1 2 ? 6.118 -6.227 27.105 1.00 49.43 ? 1 SER B CA 1 ATOM 1632 C C . SER B 1 2 ? 6.116 -4.764 27.537 1.00 47.55 ? 1 SER B C 1 ATOM 1633 O O . SER B 1 2 ? 5.731 -4.463 28.670 1.00 42.92 ? 1 SER B O 1 ATOM 1634 C CB . SER B 1 2 ? 6.531 -7.100 28.276 1.00 47.08 ? 1 SER B CB 1 ATOM 1635 O OG . SER B 1 2 ? 7.872 -6.779 28.581 1.00 51.76 ? 1 SER B OG 1 ATOM 1636 N N . ILE B 1 3 ? 6.596 -3.861 26.682 1.00 44.41 ? 2 ILE B N 1 ATOM 1637 C CA . ILE B 1 3 ? 6.538 -2.424 26.905 1.00 37.48 ? 2 ILE B CA 1 ATOM 1638 C C . ILE B 1 3 ? 5.322 -1.918 26.142 1.00 38.78 ? 2 ILE B C 1 ATOM 1639 O O . ILE B 1 3 ? 5.360 -1.812 24.915 1.00 45.45 ? 2 ILE B O 1 ATOM 1640 C CB . ILE B 1 3 ? 7.820 -1.736 26.423 1.00 37.33 ? 2 ILE B CB 1 ATOM 1641 C CG1 . ILE B 1 3 ? 9.045 -2.607 26.703 1.00 47.97 ? 2 ILE B CG1 1 ATOM 1642 C CG2 . ILE B 1 3 ? 8.023 -0.408 27.105 1.00 33.12 ? 2 ILE B CG2 1 ATOM 1643 C CD1 . ILE B 1 3 ? 9.566 -2.563 28.128 1.00 42.34 ? 2 ILE B CD1 1 ATOM 1644 N N . ILE B 1 4 ? 4.239 -1.613 26.856 1.00 37.16 ? 3 ILE B N 1 ATOM 1645 C CA . ILE B 1 4 ? 2.971 -1.246 26.225 1.00 36.66 ? 3 ILE B CA 1 ATOM 1646 C C . ILE B 1 4 ? 2.865 0.274 26.105 1.00 35.35 ? 3 ILE B C 1 ATOM 1647 O O . ILE B 1 4 ? 2.819 0.994 27.108 1.00 34.36 ? 3 ILE B O 1 ATOM 1648 C CB . ILE B 1 4 ? 1.777 -1.817 27.003 1.00 38.73 ? 3 ILE B CB 1 ATOM 1649 C CG1 . ILE B 1 4 ? 1.750 -3.345 26.938 1.00 40.34 ? 3 ILE B CG1 1 ATOM 1650 C CG2 . ILE B 1 4 ? 0.500 -1.290 26.425 1.00 37.17 ? 3 ILE B CG2 1 ATOM 1651 C CD1 . ILE B 1 4 ? 1.857 -3.894 25.527 1.00 47.49 ? 3 ILE B CD1 1 ATOM 1652 N N . VAL B 1 5 ? 2.805 0.762 24.870 1.00 34.94 ? 4 VAL B N 1 ATOM 1653 C CA . VAL B 1 5 ? 2.726 2.184 24.568 1.00 31.93 ? 4 VAL B CA 1 ATOM 1654 C C . VAL B 1 5 ? 1.794 2.366 23.378 1.00 30.27 ? 4 VAL B C 1 ATOM 1655 O O . VAL B 1 5 ? 1.502 1.424 22.647 1.00 34.32 ? 4 VAL B O 1 ATOM 1656 C CB . VAL B 1 5 ? 4.104 2.776 24.228 1.00 32.26 ? 4 VAL B CB 1 ATOM 1657 C CG1 . VAL B 1 5 ? 5.056 2.692 25.431 1.00 28.68 ? 4 VAL B CG1 1 ATOM 1658 C CG2 . VAL B 1 5 ? 4.644 2.046 23.011 1.00 31.49 ? 4 VAL B CG2 1 ATOM 1659 N N . GLU B 1 6 ? 1.352 3.598 23.167 1.00 31.62 ? 5 GLU B N 1 ATOM 1660 C CA . GLU B 1 6 ? 0.599 3.895 21.954 1.00 29.91 ? 5 GLU B CA 1 ATOM 1661 C C . GLU B 1 6 ? 1.559 4.144 20.797 1.00 32.21 ? 5 GLU B C 1 ATOM 1662 O O . GLU B 1 6 ? 2.476 4.961 20.922 1.00 29.38 ? 5 GLU B O 1 ATOM 1663 C CB . GLU B 1 6 ? -0.293 5.107 22.140 1.00 32.55 ? 5 GLU B CB 1 ATOM 1664 C CG . GLU B 1 6 ? -1.155 5.356 20.923 1.00 36.24 ? 5 GLU B CG 1 ATOM 1665 C CD . GLU B 1 6 ? -2.316 4.357 20.804 1.00 49.37 ? 5 GLU B CD 1 ATOM 1666 O OE1 . GLU B 1 6 ? -2.700 3.739 21.830 1.00 46.27 ? 5 GLU B OE1 1 ATOM 1667 O OE2 . GLU B 1 6 ? -2.856 4.204 19.684 1.00 44.76 ? 5 GLU B OE2 1 ATOM 1668 N N . PRO B 1 7 ? 1.393 3.468 19.664 1.00 34.68 ? 6 PRO B N 1 ATOM 1669 C CA . PRO B 1 7 ? 2.402 3.625 18.608 1.00 30.32 ? 6 PRO B CA 1 ATOM 1670 C C . PRO B 1 7 ? 2.407 5.002 17.976 1.00 31.25 ? 6 PRO B C 1 ATOM 1671 O O . PRO B 1 7 ? 3.479 5.511 17.623 1.00 35.41 ? 6 PRO B O 1 ATOM 1672 C CB . PRO B 1 7 ? 2.029 2.523 17.605 1.00 38.71 ? 6 PRO B CB 1 ATOM 1673 C CG . PRO B 1 7 ? 1.216 1.532 18.406 1.00 33.72 ? 6 PRO B CG 1 ATOM 1674 C CD . PRO B 1 7 ? 0.454 2.370 19.379 1.00 34.00 ? 6 PRO B CD 1 ATOM 1675 N N . HIS B 1 8 ? 1.246 5.630 17.809 1.00 34.92 ? 7 HIS B N 1 ATOM 1676 C CA . HIS B 1 8 ? 1.209 6.934 17.167 1.00 25.38 ? 7 HIS B CA 1 ATOM 1677 C C . HIS B 1 8 ? 0.240 7.833 17.900 1.00 34.60 ? 7 HIS B C 1 ATOM 1678 O O . HIS B 1 8 ? -0.839 7.398 18.304 1.00 35.52 ? 7 HIS B O 1 ATOM 1679 C CB . HIS B 1 8 ? 0.833 6.827 15.702 1.00 26.51 ? 7 HIS B CB 1 ATOM 1680 C CG . HIS B 1 8 ? 1.885 6.172 14.862 1.00 35.89 ? 7 HIS B CG 1 ATOM 1681 N ND1 . HIS B 1 8 ? 2.135 4.816 14.890 1.00 43.66 ? 7 HIS B ND1 1 ATOM 1682 C CD2 . HIS B 1 8 ? 2.792 6.702 14.009 1.00 44.38 ? 7 HIS B CD2 1 ATOM 1683 C CE1 . HIS B 1 8 ? 3.132 4.535 14.069 1.00 47.85 ? 7 HIS B CE1 1 ATOM 1684 N NE2 . HIS B 1 8 ? 3.549 5.662 13.522 1.00 49.16 ? 7 HIS B NE2 1 ATOM 1685 N N . VAL B 1 9 ? 0.654 9.082 18.096 1.00 35.38 ? 8 VAL B N 1 ATOM 1686 C CA . VAL B 1 9 ? -0.049 10.018 18.959 1.00 29.48 ? 8 VAL B CA 1 ATOM 1687 C C . VAL B 1 9 ? 0.021 11.416 18.357 1.00 32.07 ? 8 VAL B C 1 ATOM 1688 O O . VAL B 1 9 ? 1.024 11.801 17.744 1.00 30.66 ? 8 VAL B O 1 ATOM 1689 C CB . VAL B 1 9 ? 0.539 9.941 20.380 1.00 32.15 ? 8 VAL B CB 1 ATOM 1690 C CG1 . VAL B 1 9 ? 0.385 11.204 21.145 1.00 32.45 ? 8 VAL B CG1 1 ATOM 1691 C CG2 . VAL B 1 9 ? -0.084 8.799 21.121 1.00 29.24 ? 8 VAL B CG2 1 ATOM 1692 N N . THR B 1 10 ? -1.075 12.149 18.473 1.00 27.73 ? 9 THR B N 1 ATOM 1693 C CA . THR B 1 10 ? -1.085 13.551 18.112 1.00 33.49 ? 9 THR B CA 1 ATOM 1694 C C . THR B 1 10 ? -1.063 14.392 19.373 1.00 29.18 ? 9 THR B C 1 ATOM 1695 O O . THR B 1 10 ? -1.501 13.959 20.440 1.00 26.46 ? 9 THR B O 1 ATOM 1696 C CB . THR B 1 10 ? -2.302 13.933 17.252 1.00 30.46 ? 9 THR B CB 1 ATOM 1697 O OG1 . THR B 1 10 ? -3.514 13.434 17.834 1.00 42.85 ? 9 THR B OG1 1 ATOM 1698 C CG2 . THR B 1 10 ? -2.149 13.398 15.872 1.00 23.87 ? 9 THR B CG2 1 ATOM 1699 N N . ALA B 1 11 ? -0.516 15.591 19.236 1.00 32.15 ? 10 ALA B N 1 ATOM 1700 C CA . ALA B 1 11 ? -0.390 16.539 20.332 1.00 27.37 ? 10 ALA B CA 1 ATOM 1701 C C . ALA B 1 11 ? -0.710 17.931 19.816 1.00 27.13 ? 10 ALA B C 1 ATOM 1702 O O . ALA B 1 11 ? -0.172 18.361 18.792 1.00 23.70 ? 10 ALA B O 1 ATOM 1703 C CB . ALA B 1 11 ? 1.018 16.525 20.917 1.00 26.93 ? 10 ALA B CB 1 ATOM 1704 N N . VAL B 1 12 ? -1.557 18.640 20.522 1.00 24.27 ? 11 VAL B N 1 ATOM 1705 C CA . VAL B 1 12 ? -1.965 19.955 20.070 1.00 27.46 ? 11 VAL B CA 1 ATOM 1706 C C . VAL B 1 12 ? -1.048 21.014 20.663 1.00 28.24 ? 11 VAL B C 1 ATOM 1707 O O . VAL B 1 12 ? -0.836 21.067 21.880 1.00 27.89 ? 11 VAL B O 1 ATOM 1708 C CB . VAL B 1 12 ? -3.424 20.222 20.422 1.00 25.36 ? 11 VAL B CB 1 ATOM 1709 C CG1 . VAL B 1 12 ? -3.777 21.589 19.941 1.00 20.76 ? 11 VAL B CG1 1 ATOM 1710 C CG2 . VAL B 1 12 ? -4.257 19.159 19.749 1.00 22.68 ? 11 VAL B CG2 1 ATOM 1711 N N . TRP B 1 13 ? -0.525 21.864 19.786 1.00 21.97 ? 12 TRP B N 1 ATOM 1712 C CA . TRP B 1 13 ? 0.371 22.930 20.161 1.00 18.77 ? 12 TRP B CA 1 ATOM 1713 C C . TRP B 1 13 ? -0.185 23.709 21.333 1.00 22.83 ? 12 TRP B C 1 ATOM 1714 O O . TRP B 1 13 ? -1.330 24.171 21.293 1.00 30.93 ? 12 TRP B O 1 ATOM 1715 C CB . TRP B 1 13 ? 0.564 23.848 18.958 1.00 20.75 ? 12 TRP B CB 1 ATOM 1716 C CG . TRP B 1 13 ? 1.694 24.791 19.100 1.00 23.18 ? 12 TRP B CG 1 ATOM 1717 C CD1 . TRP B 1 13 ? 2.977 24.602 18.671 1.00 22.47 ? 12 TRP B CD1 1 ATOM 1718 C CD2 . TRP B 1 13 ? 1.666 26.074 19.735 1.00 25.77 ? 12 TRP B CD2 1 ATOM 1719 N NE1 . TRP B 1 13 ? 3.746 25.702 18.987 1.00 21.81 ? 12 TRP B NE1 1 ATOM 1720 C CE2 . TRP B 1 13 ? 2.972 26.614 19.646 1.00 20.79 ? 12 TRP B CE2 1 ATOM 1721 C CE3 . TRP B 1 13 ? 0.669 26.819 20.369 1.00 26.76 ? 12 TRP B CE3 1 ATOM 1722 C CZ2 . TRP B 1 13 ? 3.300 27.864 20.165 1.00 20.80 ? 12 TRP B CZ2 1 ATOM 1723 C CZ3 . TRP B 1 13 ? 0.998 28.064 20.888 1.00 23.50 ? 12 TRP B CZ3 1 ATOM 1724 C CH2 . TRP B 1 13 ? 2.301 28.571 20.783 1.00 20.98 ? 12 TRP B CH2 1 ATOM 1725 N N . GLY B 1 14 ? 0.632 23.859 22.375 1.00 22.79 ? 13 GLY B N 1 ATOM 1726 C CA . GLY B 1 14 ? 0.276 24.665 23.528 1.00 21.77 ? 13 GLY B CA 1 ATOM 1727 C C . GLY B 1 14 ? -0.683 24.010 24.500 1.00 29.52 ? 13 GLY B C 1 ATOM 1728 O O . GLY B 1 14 ? -1.122 24.662 25.463 1.00 23.18 ? 13 GLY B O 1 ATOM 1729 N N . LYS B 1 15 ? -1.036 22.749 24.278 1.00 27.80 ? 14 LYS B N 1 ATOM 1730 C CA . LYS B 1 15 ? -1.807 22.003 25.238 1.00 30.92 ? 14 LYS B CA 1 ATOM 1731 C C . LYS B 1 15 ? -0.951 20.865 25.807 1.00 29.51 ? 14 LYS B C 1 ATOM 1732 O O . LYS B 1 15 ? 0.286 20.948 25.797 1.00 36.49 ? 14 LYS B O 1 ATOM 1733 C CB . LYS B 1 15 ? -3.091 21.546 24.560 1.00 26.91 ? 14 LYS B CB 1 ATOM 1734 C CG . LYS B 1 15 ? -3.996 22.693 24.225 1.00 26.30 ? 14 LYS B CG 1 ATOM 1735 C CD . LYS B 1 15 ? -5.182 22.193 23.398 1.00 36.58 ? 14 LYS B CD 1 ATOM 1736 C CE . LYS B 1 15 ? -6.245 23.262 23.202 1.00 42.04 ? 14 LYS B CE 1 ATOM 1737 N NZ . LYS B 1 15 ? -6.824 23.724 24.502 1.00 41.86 ? 14 LYS B NZ 1 ATOM 1738 N N . ASN B 1 16 ? -1.612 19.814 26.296 1.00 32.61 ? 15 ASN B N 1 ATOM 1739 C CA . ASN B 1 16 ? -1.014 18.658 26.950 1.00 32.63 ? 15 ASN B CA 1 ATOM 1740 C C . ASN B 1 16 ? -1.165 17.413 26.090 1.00 37.25 ? 15 ASN B C 1 ATOM 1741 O O . ASN B 1 16 ? -2.056 17.330 25.237 1.00 35.84 ? 15 ASN B O 1 ATOM 1742 C CB . ASN B 1 16 ? -1.698 18.372 28.285 1.00 23.80 ? 15 ASN B CB 1 ATOM 1743 C CG . ASN B 1 16 ? -1.978 19.610 29.061 1.00 41.81 ? 15 ASN B CG 1 ATOM 1744 O OD1 . ASN B 1 16 ? -1.217 20.584 29.009 1.00 42.86 ? 15 ASN B OD1 1 ATOM 1745 N ND2 . ASN B 1 16 ? -3.088 19.598 29.794 1.00 50.50 ? 15 ASN B ND2 1 ATOM 1746 N N . VAL B 1 17 ? -0.320 16.417 26.375 1.00 29.66 ? 16 VAL B N 1 ATOM 1747 C CA . VAL B 1 17 ? -0.455 15.077 25.817 1.00 27.75 ? 16 VAL B CA 1 ATOM 1748 C C . VAL B 1 17 ? 0.142 14.075 26.791 1.00 32.60 ? 16 VAL B C 1 ATOM 1749 O O . VAL B 1 17 ? 1.125 14.353 27.476 1.00 31.96 ? 16 VAL B O 1 ATOM 1750 C CB . VAL B 1 17 ? 0.223 14.924 24.436 1.00 32.79 ? 16 VAL B CB 1 ATOM 1751 C CG1 . VAL B 1 17 ? 1.745 15.004 24.543 1.00 31.43 ? 16 VAL B CG1 1 ATOM 1752 C CG2 . VAL B 1 17 ? -0.182 13.600 23.810 1.00 25.48 ? 16 VAL B CG2 1 ATOM 1753 N N . SER B 1 18 ? -0.443 12.892 26.822 1.00 27.94 ? 17 SER B N 1 ATOM 1754 C CA . SER B 1 18 ? -0.015 11.832 27.711 1.00 28.15 ? 17 SER B CA 1 ATOM 1755 C C . SER B 1 18 ? 0.797 10.818 26.918 1.00 33.33 ? 17 SER B C 1 ATOM 1756 O O . SER B 1 18 ? 0.330 10.313 25.895 1.00 35.19 ? 17 SER B O 1 ATOM 1757 C CB . SER B 1 18 ? -1.221 11.166 28.354 1.00 22.74 ? 17 SER B CB 1 ATOM 1758 O OG . SER B 1 18 ? -0.810 10.154 29.245 1.00 36.67 ? 17 SER B OG 1 ATOM 1759 N N . LEU B 1 19 ? 2.004 10.523 27.382 1.00 23.60 ? 18 LEU B N 1 ATOM 1760 C CA . LEU B 1 19 ? 2.836 9.509 26.755 1.00 23.64 ? 18 LEU B CA 1 ATOM 1761 C C . LEU B 1 19 ? 2.723 8.265 27.631 1.00 26.39 ? 18 LEU B C 1 ATOM 1762 O O . LEU B 1 19 ? 3.399 8.138 28.655 1.00 29.63 ? 18 LEU B O 1 ATOM 1763 C CB . LEU B 1 19 ? 4.276 9.988 26.596 1.00 29.12 ? 18 LEU B CB 1 ATOM 1764 C CG . LEU B 1 19 ? 4.508 11.177 25.660 1.00 26.85 ? 18 LEU B CG 1 ATOM 1765 C CD1 . LEU B 1 19 ? 5.940 11.245 25.259 1.00 23.82 ? 18 LEU B CD1 1 ATOM 1766 C CD2 . LEU B 1 19 ? 3.641 11.046 24.438 1.00 38.78 ? 18 LEU B CD2 1 ATOM 1767 N N . LYS B 1 20 ? 1.864 7.350 27.217 1.00 26.64 ? 19 LYS B N 1 ATOM 1768 C CA . LYS B 1 20 ? 1.511 6.196 28.025 1.00 30.61 ? 19 LYS B CA 1 ATOM 1769 C C . LYS B 1 20 ? 2.589 5.118 27.914 1.00 27.14 ? 19 LYS B C 1 ATOM 1770 O O . LYS B 1 20 ? 3.130 4.877 26.833 1.00 31.86 ? 19 LYS B O 1 ATOM 1771 C CB . LYS B 1 20 ? 0.144 5.671 27.564 1.00 31.11 ? 19 LYS B CB 1 ATOM 1772 C CG . LYS B 1 20 ? -0.253 4.332 28.121 1.00 37.06 ? 19 LYS B CG 1 ATOM 1773 C CD . LYS B 1 20 ? -1.345 3.687 27.292 1.00 43.70 ? 19 LYS B CD 1 ATOM 1774 C CE . LYS B 1 20 ? -1.636 2.268 27.775 1.00 53.49 ? 19 LYS B CE 1 ATOM 1775 N NZ . LYS B 1 20 ? -2.746 1.616 27.018 1.00 57.92 ? 19 LYS B NZ 1 ATOM 1776 N N . CYS B 1 21 ? 2.929 4.488 29.043 1.00 25.97 ? 20 CYS B N 1 ATOM 1777 C CA . CYS B 1 21 ? 3.871 3.361 29.016 1.00 27.66 ? 20 CYS B CA 1 ATOM 1778 C C . CYS B 1 21 ? 3.631 2.464 30.224 1.00 26.04 ? 20 CYS B C 1 ATOM 1779 O O . CYS B 1 21 ? 3.825 2.890 31.363 1.00 29.02 ? 20 CYS B O 1 ATOM 1780 C CB . CYS B 1 21 ? 5.318 3.852 28.976 1.00 29.04 ? 20 CYS B CB 1 ATOM 1781 S SG . CYS B 1 21 ? 6.532 2.544 28.730 1.00 31.77 ? 20 CYS B SG 1 ATOM 1782 N N . LEU B 1 22 ? 3.208 1.233 29.978 1.00 29.60 ? 21 LEU B N 1 ATOM 1783 C CA . LEU B 1 22 ? 3.058 0.225 31.022 1.00 37.65 ? 21 LEU B CA 1 ATOM 1784 C C . LEU B 1 22 ? 4.095 -0.873 30.844 1.00 39.77 ? 21 LEU B C 1 ATOM 1785 O O . LEU B 1 22 ? 4.296 -1.373 29.733 1.00 38.83 ? 21 LEU B O 1 ATOM 1786 C CB . LEU B 1 22 ? 1.671 -0.401 30.993 1.00 32.91 ? 21 LEU B CB 1 ATOM 1787 C CG . LEU B 1 22 ? 0.572 0.627 30.946 1.00 38.53 ? 21 LEU B CG 1 ATOM 1788 C CD1 . LEU B 1 22 ? -0.699 -0.037 30.455 1.00 40.45 ? 21 LEU B CD1 1 ATOM 1789 C CD2 . LEU B 1 22 ? 0.479 1.210 32.335 1.00 34.22 ? 21 LEU B CD2 1 ATOM 1790 N N . ILE B 1 23 ? 4.740 -1.259 31.940 1.00 38.39 ? 22 ILE B N 1 ATOM 1791 C CA . ILE B 1 23 ? 5.897 -2.150 31.895 1.00 46.23 ? 22 ILE B CA 1 ATOM 1792 C C . ILE B 1 23 ? 5.519 -3.455 32.577 1.00 39.47 ? 22 ILE B C 1 ATOM 1793 O O . ILE B 1 23 ? 5.451 -3.525 33.809 1.00 31.50 ? 22 ILE B O 1 ATOM 1794 C CB . ILE B 1 23 ? 7.120 -1.514 32.560 1.00 40.69 ? 22 ILE B CB 1 ATOM 1795 C CG1 . ILE B 1 23 ? 7.317 -0.128 32.006 1.00 26.30 ? 22 ILE B CG1 1 ATOM 1796 C CG2 . ILE B 1 23 ? 8.383 -2.330 32.315 1.00 40.44 ? 22 ILE B CG2 1 ATOM 1797 C CD1 . ILE B 1 23 ? 8.221 0.668 32.838 1.00 25.29 ? 22 ILE B CD1 1 ATOM 1798 N N . GLU B 1 24 ? 5.275 -4.484 31.781 1.00 41.69 ? 23 GLU B N 1 ATOM 1799 C CA . GLU B 1 24 ? 4.922 -5.783 32.335 1.00 55.03 ? 23 GLU B CA 1 ATOM 1800 C C . GLU B 1 24 ? 5.986 -6.832 32.025 1.00 54.11 ? 23 GLU B C 1 ATOM 1801 O O . GLU B 1 24 ? 5.702 -7.823 31.348 1.00 53.63 ? 23 GLU B O 1 ATOM 1802 C CB . GLU B 1 24 ? 3.559 -6.206 31.794 1.00 52.81 ? 23 GLU B CB 1 ATOM 1803 C CG . GLU B 1 24 ? 2.465 -5.229 32.161 1.00 56.32 ? 23 GLU B CG 1 ATOM 1804 C CD . GLU B 1 24 ? 1.099 -5.645 31.660 1.00 63.62 ? 23 GLU B CD 1 ATOM 1805 O OE1 . GLU B 1 24 ? 1.032 -6.380 30.655 1.00 51.51 ? 23 GLU B OE1 1 ATOM 1806 O OE2 . GLU B 1 24 ? 0.087 -5.239 32.280 1.00 79.26 ? 23 GLU B OE2 1 ATOM 1807 N N . VAL B 1 25 ? 7.211 -6.622 32.518 1.00 55.70 ? 24 VAL B N 1 ATOM 1808 C CA . VAL B 1 25 ? 8.336 -7.497 32.180 1.00 59.31 ? 24 VAL B CA 1 ATOM 1809 C C . VAL B 1 25 ? 8.470 -8.698 33.118 1.00 65.01 ? 24 VAL B C 1 ATOM 1810 O O . VAL B 1 25 ? 9.097 -9.701 32.735 1.00 64.41 ? 24 VAL B O 1 ATOM 1811 C CB . VAL B 1 25 ? 9.673 -6.724 32.156 1.00 46.92 ? 24 VAL B CB 1 ATOM 1812 C CG1 . VAL B 1 25 ? 9.692 -5.669 31.065 1.00 37.17 ? 24 VAL B CG1 1 ATOM 1813 C CG2 . VAL B 1 25 ? 9.931 -6.074 33.490 1.00 42.64 ? 24 VAL B CG2 1 ATOM 1814 N N . ASN B 1 26 ? 7.897 -8.633 34.328 1.00 62.54 ? 25 ASN B N 1 ATOM 1815 C CA . ASN B 1 26 ? 7.992 -9.718 35.313 1.00 63.76 ? 25 ASN B CA 1 ATOM 1816 C C . ASN B 1 26 ? 9.442 -9.985 35.692 1.00 57.40 ? 25 ASN B C 1 ATOM 1817 O O . ASN B 1 26 ? 9.836 -11.119 36.001 1.00 59.63 ? 25 ASN B O 1 ATOM 1818 C CB . ASN B 1 26 ? 7.293 -10.980 34.800 1.00 64.32 ? 25 ASN B CB 1 ATOM 1819 C CG . ASN B 1 26 ? 5.791 -10.784 34.671 1.00 78.03 ? 25 ASN B CG 1 ATOM 1820 O OD1 . ASN B 1 26 ? 5.211 -9.908 35.328 1.00 77.35 ? 25 ASN B OD1 1 ATOM 1821 N ND2 . ASN B 1 26 ? 5.156 -11.576 33.812 1.00 82.26 ? 25 ASN B ND2 1 ATOM 1822 N N . GLU B 1 27 ? 10.216 -8.908 35.692 1.00 56.15 ? 26 GLU B N 1 ATOM 1823 C CA . GLU B 1 27 ? 11.651 -8.881 35.864 1.00 45.58 ? 26 GLU B CA 1 ATOM 1824 C C . GLU B 1 27 ? 11.954 -7.814 36.910 1.00 45.91 ? 26 GLU B C 1 ATOM 1825 O O . GLU B 1 27 ? 11.093 -6.989 37.226 1.00 53.85 ? 26 GLU B O 1 ATOM 1826 C CB . GLU B 1 27 ? 12.296 -8.557 34.527 1.00 45.54 ? 26 GLU B CB 1 ATOM 1827 C CG . GLU B 1 27 ? 13.742 -8.352 34.589 1.00 54.29 ? 26 GLU B CG 1 ATOM 1828 C CD . GLU B 1 27 ? 14.462 -9.086 33.511 1.00 63.91 ? 26 GLU B CD 1 ATOM 1829 O OE1 . GLU B 1 27 ? 13.796 -9.774 32.702 1.00 73.72 ? 26 GLU B OE1 1 ATOM 1830 O OE2 . GLU B 1 27 ? 15.685 -8.853 33.387 1.00 63.23 ? 26 GLU B OE2 1 ATOM 1831 N N . THR B 1 28 ? 13.166 -7.810 37.474 1.00 47.38 ? 27 THR B N 1 ATOM 1832 C CA . THR B 1 28 ? 13.540 -6.712 38.359 1.00 41.05 ? 27 THR B CA 1 ATOM 1833 C C . THR B 1 28 ? 13.812 -5.446 37.542 1.00 40.61 ? 27 THR B C 1 ATOM 1834 O O . THR B 1 28 ? 14.628 -5.451 36.612 1.00 37.51 ? 27 THR B O 1 ATOM 1835 C CB . THR B 1 28 ? 14.771 -7.059 39.195 1.00 43.78 ? 27 THR B CB 1 ATOM 1836 O OG1 . THR B 1 28 ? 14.690 -8.402 39.685 1.00 45.87 ? 27 THR B OG1 1 ATOM 1837 C CG2 . THR B 1 28 ? 14.862 -6.107 40.373 1.00 40.04 ? 27 THR B CG2 1 ATOM 1838 N N . ILE B 1 29 ? 13.128 -4.356 37.884 1.00 37.50 ? 28 ILE B N 1 ATOM 1839 C CA . ILE B 1 29 ? 13.269 -3.098 37.157 1.00 36.37 ? 28 ILE B CA 1 ATOM 1840 C C . ILE B 1 29 ? 14.407 -2.309 37.779 1.00 27.45 ? 28 ILE B C 1 ATOM 1841 O O . ILE B 1 29 ? 14.374 -1.978 38.967 1.00 32.31 ? 28 ILE B O 1 ATOM 1842 C CB . ILE B 1 29 ? 11.959 -2.288 37.152 1.00 43.30 ? 28 ILE B CB 1 ATOM 1843 C CG1 . ILE B 1 29 ? 10.845 -3.051 36.426 1.00 36.90 ? 28 ILE B CG1 1 ATOM 1844 C CG2 . ILE B 1 29 ? 12.150 -0.946 36.441 1.00 34.23 ? 28 ILE B CG2 1 ATOM 1845 C CD1 . ILE B 1 29 ? 11.083 -3.167 34.954 1.00 36.91 ? 28 ILE B CD1 1 ATOM 1846 N N . THR B 1 30 ? 15.434 -2.043 36.981 1.00 33.45 ? 29 THR B N 1 ATOM 1847 C CA . THR B 1 30 ? 16.535 -1.205 37.429 1.00 27.11 ? 29 THR B CA 1 ATOM 1848 C C . THR B 1 30 ? 16.177 0.275 37.322 1.00 33.28 ? 29 THR B C 1 ATOM 1849 O O . THR B 1 30 ? 16.244 1.010 38.309 1.00 36.50 ? 29 THR B O 1 ATOM 1850 C CB . THR B 1 30 ? 17.775 -1.533 36.612 1.00 31.28 ? 29 THR B CB 1 ATOM 1851 O OG1 . THR B 1 30 ? 18.094 -2.904 36.819 1.00 38.11 ? 29 THR B OG1 1 ATOM 1852 C CG2 . THR B 1 30 ? 18.945 -0.721 37.060 1.00 31.19 ? 29 THR B CG2 1 ATOM 1853 N N . GLN B 1 31 ? 15.777 0.729 36.139 1.00 30.38 ? 30 GLN B N 1 ATOM 1854 C CA . GLN B 1 31 ? 15.266 2.078 35.975 1.00 21.30 ? 30 GLN B CA 1 ATOM 1855 C C . GLN B 1 31 ? 14.464 2.131 34.686 1.00 30.14 ? 30 GLN B C 1 ATOM 1856 O O . GLN B 1 31 ? 14.578 1.251 33.827 1.00 32.49 ? 30 GLN B O 1 ATOM 1857 C CB . GLN B 1 31 ? 16.394 3.101 35.949 1.00 22.27 ? 30 GLN B CB 1 ATOM 1858 C CG . GLN B 1 31 ? 17.037 3.287 34.606 1.00 19.22 ? 30 GLN B CG 1 ATOM 1859 C CD . GLN B 1 31 ? 18.217 4.221 34.692 1.00 28.66 ? 30 GLN B CD 1 ATOM 1860 O OE1 . GLN B 1 31 ? 18.726 4.476 35.780 1.00 30.41 ? 30 GLN B OE1 1 ATOM 1861 N NE2 . GLN B 1 31 ? 18.668 4.737 33.551 1.00 28.84 ? 30 GLN B NE2 1 ATOM 1862 N N . ILE B 1 32 ? 13.641 3.174 34.564 1.00 27.67 ? 31 ILE B N 1 ATOM 1863 C CA . ILE B 1 32 ? 12.767 3.374 33.413 1.00 28.66 ? 31 ILE B CA 1 ATOM 1864 C C . ILE B 1 32 ? 12.963 4.795 32.899 1.00 26.29 ? 31 ILE B C 1 ATOM 1865 O O . ILE B 1 32 ? 13.279 5.716 33.656 1.00 27.85 ? 31 ILE B O 1 ATOM 1866 C CB . ILE B 1 32 ? 11.273 3.082 33.763 1.00 23.92 ? 31 ILE B CB 1 ATOM 1867 C CG1 . ILE B 1 32 ? 10.733 4.075 34.784 1.00 27.73 ? 31 ILE B CG1 1 ATOM 1868 C CG2 . ILE B 1 32 ? 11.149 1.724 34.390 1.00 24.57 ? 31 ILE B CG2 1 ATOM 1869 C CD1 . ILE B 1 32 ? 9.371 3.686 35.420 1.00 25.51 ? 31 ILE B CD1 1 ATOM 1870 N N . SER B 1 33 ? 12.784 4.973 31.599 1.00 30.06 ? 32 SER B N 1 ATOM 1871 C CA . SER B 1 33 ? 13.051 6.275 31.020 1.00 25.10 ? 32 SER B CA 1 ATOM 1872 C C . SER B 1 33 ? 12.287 6.450 29.710 1.00 33.37 ? 32 SER B C 1 ATOM 1873 O O . SER B 1 33 ? 11.975 5.477 29.016 1.00 28.04 ? 32 SER B O 1 ATOM 1874 C CB . SER B 1 33 ? 14.536 6.449 30.768 1.00 23.81 ? 32 SER B CB 1 ATOM 1875 O OG . SER B 1 33 ? 14.849 5.820 29.550 1.00 34.20 ? 32 SER B OG 1 ATOM 1876 N N . TRP B 1 34 ? 11.998 7.720 29.385 1.00 27.65 ? 33 TRP B N 1 ATOM 1877 C CA . TRP B 1 34 ? 11.601 8.160 28.053 1.00 23.85 ? 33 TRP B CA 1 ATOM 1878 C C . TRP B 1 34 ? 12.769 8.879 27.388 1.00 27.84 ? 33 TRP B C 1 ATOM 1879 O O . TRP B 1 34 ? 13.424 9.730 28.008 1.00 30.08 ? 33 TRP B O 1 ATOM 1880 C CB . TRP B 1 34 ? 10.399 9.111 28.116 1.00 21.88 ? 33 TRP B CB 1 ATOM 1881 C CG . TRP B 1 34 ? 9.061 8.456 28.252 1.00 23.86 ? 33 TRP B CG 1 ATOM 1882 C CD1 . TRP B 1 34 ? 8.307 8.339 29.396 1.00 19.54 ? 33 TRP B CD1 1 ATOM 1883 C CD2 . TRP B 1 34 ? 8.305 7.837 27.211 1.00 20.54 ? 33 TRP B CD2 1 ATOM 1884 N NE1 . TRP B 1 34 ? 7.141 7.680 29.120 1.00 19.87 ? 33 TRP B NE1 1 ATOM 1885 C CE2 . TRP B 1 34 ? 7.111 7.363 27.788 1.00 20.72 ? 33 TRP B CE2 1 ATOM 1886 C CE3 . TRP B 1 34 ? 8.525 7.628 25.845 1.00 23.35 ? 33 TRP B CE3 1 ATOM 1887 C CZ2 . TRP B 1 34 ? 6.133 6.709 27.045 1.00 27.31 ? 33 TRP B CZ2 1 ATOM 1888 C CZ3 . TRP B 1 34 ? 7.559 6.965 25.113 1.00 24.66 ? 33 TRP B CZ3 1 ATOM 1889 C CH2 . TRP B 1 34 ? 6.378 6.517 25.713 1.00 26.37 ? 33 TRP B CH2 1 ATOM 1890 N N . GLU B 1 35 ? 13.010 8.572 26.117 1.00 29.58 ? 34 GLU B N 1 ATOM 1891 C CA . GLU B 1 35 ? 14.074 9.214 25.339 1.00 38.01 ? 34 GLU B CA 1 ATOM 1892 C C . GLU B 1 35 ? 13.542 9.662 23.983 1.00 28.04 ? 34 GLU B C 1 ATOM 1893 O O . GLU B 1 35 ? 12.499 9.200 23.527 1.00 29.28 ? 34 GLU B O 1 ATOM 1894 C CB . GLU B 1 35 ? 15.281 8.277 25.145 1.00 36.14 ? 34 GLU B CB 1 ATOM 1895 C CG . GLU B 1 35 ? 15.858 7.793 26.460 1.00 36.64 ? 34 GLU B CG 1 ATOM 1896 C CD . GLU B 1 35 ? 16.924 6.746 26.293 1.00 45.19 ? 34 GLU B CD 1 ATOM 1897 O OE1 . GLU B 1 35 ? 17.173 6.345 25.135 1.00 46.48 ? 34 GLU B OE1 1 ATOM 1898 O OE2 . GLU B 1 35 ? 17.502 6.323 27.326 1.00 54.86 ? 34 GLU B OE2 1 ATOM 1899 N N . LYS B 1 36 ? 14.261 10.583 23.341 1.00 36.48 ? 35 LYS B N 1 ATOM 1900 C CA . LYS B 1 36 ? 13.872 11.111 22.036 1.00 37.50 ? 35 LYS B CA 1 ATOM 1901 C C . LYS B 1 36 ? 14.976 10.871 21.018 1.00 43.82 ? 35 LYS B C 1 ATOM 1902 O O . LYS B 1 36 ? 16.146 11.145 21.299 1.00 50.70 ? 35 LYS B O 1 ATOM 1903 C CB . LYS B 1 36 ? 13.563 12.605 22.114 1.00 38.94 ? 35 LYS B CB 1 ATOM 1904 C CG . LYS B 1 36 ? 12.980 13.189 20.828 1.00 38.84 ? 35 LYS B CG 1 ATOM 1905 C CD . LYS B 1 36 ? 12.224 14.466 21.109 1.00 35.29 ? 35 LYS B CD 1 ATOM 1906 C CE . LYS B 1 36 ? 11.468 14.969 19.889 1.00 37.05 ? 35 LYS B CE 1 ATOM 1907 N NZ . LYS B 1 36 ? 12.401 15.386 18.801 1.00 47.71 ? 35 LYS B NZ 1 ATOM 1908 N N . ILE B 1 37 ? 14.602 10.383 19.830 1.00 43.30 ? 36 ILE B N 1 ATOM 1909 C CA . ILE B 1 37 ? 15.577 10.133 18.766 1.00 48.50 ? 36 ILE B CA 1 ATOM 1910 C C . ILE B 1 37 ? 16.082 11.457 18.202 1.00 53.13 ? 36 ILE B C 1 ATOM 1911 O O . ILE B 1 37 ? 15.298 12.375 17.928 1.00 52.29 ? 36 ILE B O 1 ATOM 1912 C CB . ILE B 1 37 ? 14.966 9.250 17.664 1.00 42.89 ? 36 ILE B CB 1 ATOM 1913 C CG1 . ILE B 1 37 ? 15.133 7.784 18.008 1.00 42.59 ? 36 ILE B CG1 1 ATOM 1914 C CG2 . ILE B 1 37 ? 15.631 9.467 16.321 1.00 36.87 ? 36 ILE B CG2 1 ATOM 1915 C CD1 . ILE B 1 37 ? 14.340 7.346 19.169 1.00 41.73 ? 36 ILE B CD1 1 ATOM 1916 N N . HIS B 1 38 ? 17.405 11.560 18.033 1.00 59.32 ? 37 HIS B N 1 ATOM 1917 C CA . HIS B 1 38 ? 18.051 12.717 17.401 1.00 60.05 ? 37 HIS B CA 1 ATOM 1918 C C . HIS B 1 38 ? 19.189 12.177 16.541 1.00 64.15 ? 37 HIS B C 1 ATOM 1919 O O . HIS B 1 38 ? 20.281 11.905 17.048 1.00 74.25 ? 37 HIS B O 1 ATOM 1920 C CB . HIS B 1 38 ? 18.563 13.703 18.440 1.00 60.56 ? 37 HIS B CB 1 ATOM 1921 C CG . HIS B 1 38 ? 17.477 14.424 19.174 1.00 59.76 ? 37 HIS B CG 1 ATOM 1922 N ND1 . HIS B 1 38 ? 17.519 14.649 20.533 1.00 52.57 ? 37 HIS B ND1 1 ATOM 1923 C CD2 . HIS B 1 38 ? 16.326 14.985 18.734 1.00 61.51 ? 37 HIS B CD2 1 ATOM 1924 C CE1 . HIS B 1 38 ? 16.435 15.308 20.903 1.00 56.16 ? 37 HIS B CE1 1 ATOM 1925 N NE2 . HIS B 1 38 ? 15.694 15.523 19.830 1.00 63.99 ? 37 HIS B NE2 1 ATOM 1926 N N . GLY B 1 39 ? 18.933 12.029 15.248 1.00 67.67 ? 38 GLY B N 1 ATOM 1927 C CA . GLY B 1 39 ? 19.877 11.315 14.404 1.00 67.82 ? 38 GLY B CA 1 ATOM 1928 C C . GLY B 1 39 ? 19.884 9.857 14.811 1.00 68.22 ? 38 GLY B C 1 ATOM 1929 O O . GLY B 1 39 ? 18.831 9.227 14.954 1.00 69.37 ? 38 GLY B O 1 ATOM 1930 N N . LYS B 1 40 ? 21.074 9.304 15.018 1.00 68.11 ? 39 LYS B N 1 ATOM 1931 C CA . LYS B 1 40 ? 21.146 7.997 15.655 1.00 78.55 ? 39 LYS B CA 1 ATOM 1932 C C . LYS B 1 40 ? 21.206 8.112 17.176 1.00 79.39 ? 39 LYS B C 1 ATOM 1933 O O . LYS B 1 40 ? 20.663 7.250 17.876 1.00 85.16 ? 39 LYS B O 1 ATOM 1934 C CB . LYS B 1 40 ? 22.344 7.208 15.103 1.00 80.88 ? 39 LYS B CB 1 ATOM 1935 C CG . LYS B 1 40 ? 22.568 5.768 15.646 1.00 82.67 ? 39 LYS B CG 1 ATOM 1936 C CD . LYS B 1 40 ? 21.315 5.026 16.168 1.00 85.31 ? 39 LYS B CD 1 ATOM 1937 C CE . LYS B 1 40 ? 20.390 4.475 15.095 1.00 77.45 ? 39 LYS B CE 1 ATOM 1938 N NZ . LYS B 1 40 ? 19.055 4.170 15.695 1.00 75.09 ? 39 LYS B NZ 1 ATOM 1939 N N . SER B 1 41 ? 21.803 9.173 17.712 1.00 71.55 ? 40 SER B N 1 ATOM 1940 C CA . SER B 1 41 ? 21.799 9.343 19.155 1.00 67.55 ? 40 SER B CA 1 ATOM 1941 C C . SER B 1 41 ? 20.381 9.568 19.657 1.00 65.46 ? 40 SER B C 1 ATOM 1942 O O . SER B 1 41 ? 19.490 9.991 18.918 1.00 61.51 ? 40 SER B O 1 ATOM 1943 C CB . SER B 1 41 ? 22.664 10.527 19.577 1.00 72.59 ? 40 SER B CB 1 ATOM 1944 O OG . SER B 1 41 ? 22.150 11.741 19.050 1.00 75.83 ? 40 SER B OG 1 ATOM 1945 N N . THR B 1 42 ? 20.184 9.278 20.938 1.00 61.67 ? 41 THR B N 1 ATOM 1946 C CA . THR B 1 42 ? 18.949 9.588 21.634 1.00 54.55 ? 41 THR B CA 1 ATOM 1947 C C . THR B 1 42 ? 19.259 10.490 22.816 1.00 52.25 ? 41 THR B C 1 ATOM 1948 O O . THR B 1 42 ? 20.354 10.450 23.379 1.00 54.03 ? 41 THR B O 1 ATOM 1949 C CB . THR B 1 42 ? 18.232 8.328 22.123 1.00 56.73 ? 41 THR B CB 1 ATOM 1950 O OG1 . THR B 1 42 ? 18.894 7.829 23.290 1.00 65.63 ? 41 THR B OG1 1 ATOM 1951 C CG2 . THR B 1 42 ? 18.237 7.252 21.037 1.00 59.69 ? 41 THR B CG2 1 ATOM 1952 N N . GLN B 1 43 ? 18.285 11.315 23.173 1.00 54.71 ? 42 GLN B N 1 ATOM 1953 C CA . GLN B 1 43 ? 18.387 12.229 24.298 1.00 48.22 ? 42 GLN B CA 1 ATOM 1954 C C . GLN B 1 43 ? 17.290 11.905 25.297 1.00 41.27 ? 42 GLN B C 1 ATOM 1955 O O . GLN B 1 43 ? 16.180 11.534 24.911 1.00 43.38 ? 42 GLN B O 1 ATOM 1956 C CB . GLN B 1 43 ? 18.303 13.682 23.830 1.00 47.12 ? 42 GLN B CB 1 ATOM 1957 C CG . GLN B 1 43 ? 19.558 14.091 23.065 1.00 59.74 ? 42 GLN B CG 1 ATOM 1958 C CD . GLN B 1 43 ? 19.571 15.548 22.721 1.00 63.99 ? 42 GLN B CD 1 ATOM 1959 O OE1 . GLN B 1 43 ? 18.539 16.217 22.794 1.00 61.48 ? 42 GLN B OE1 1 ATOM 1960 N NE2 . GLN B 1 43 ? 20.738 16.058 22.336 1.00 68.80 ? 42 GLN B NE2 1 ATOM 1961 N N . THR B 1 44 ? 17.622 12.026 26.579 1.00 45.66 ? 43 THR B N 1 ATOM 1962 C CA . THR B 1 44 ? 16.734 11.619 27.661 1.00 34.80 ? 43 THR B CA 1 ATOM 1963 C C . THR B 1 44 ? 15.643 12.653 27.898 1.00 32.78 ? 43 THR B C 1 ATOM 1964 O O . THR B 1 44 ? 15.913 13.853 27.962 1.00 34.33 ? 43 THR B O 1 ATOM 1965 C CB . THR B 1 44 ? 17.537 11.422 28.946 1.00 34.41 ? 43 THR B CB 1 ATOM 1966 O OG1 . THR B 1 44 ? 18.544 10.433 28.730 1.00 49.36 ? 43 THR B OG1 1 ATOM 1967 C CG2 . THR B 1 44 ? 16.656 10.993 30.087 1.00 28.88 ? 43 THR B CG2 1 ATOM 1968 N N . VAL B 1 45 ? 14.405 12.186 28.038 1.00 29.89 ? 44 VAL B N 1 ATOM 1969 C CA . VAL B 1 45 ? 13.331 13.098 28.391 1.00 28.90 ? 44 VAL B CA 1 ATOM 1970 C C . VAL B 1 45 ? 13.102 13.024 29.891 1.00 28.00 ? 44 VAL B C 1 ATOM 1971 O O . VAL B 1 45 ? 13.184 14.047 30.575 1.00 29.64 ? 44 VAL B O 1 ATOM 1972 C CB . VAL B 1 45 ? 12.041 12.808 27.598 1.00 29.92 ? 44 VAL B CB 1 ATOM 1973 C CG1 . VAL B 1 45 ? 10.860 13.613 28.168 1.00 17.14 ? 44 VAL B CG1 1 ATOM 1974 C CG2 . VAL B 1 45 ? 12.254 13.162 26.140 1.00 26.58 ? 44 VAL B CG2 1 ATOM 1975 N N . ALA B 1 46 ? 12.848 11.824 30.420 1.00 24.11 ? 45 ALA B N 1 ATOM 1976 C CA . ALA B 1 46 ? 12.594 11.654 31.845 1.00 16.93 ? 45 ALA B CA 1 ATOM 1977 C C . ALA B 1 46 ? 13.039 10.268 32.274 1.00 23.26 ? 45 ALA B C 1 ATOM 1978 O O . ALA B 1 46 ? 12.961 9.313 31.504 1.00 24.89 ? 45 ALA B O 1 ATOM 1979 C CB . ALA B 1 46 ? 11.109 11.850 32.193 1.00 23.49 ? 45 ALA B CB 1 ATOM 1980 N N . VAL B 1 47 ? 13.487 10.173 33.524 1.00 26.13 ? 46 VAL B N 1 ATOM 1981 C CA . VAL B 1 47 ? 14.080 8.974 34.104 1.00 21.42 ? 46 VAL B CA 1 ATOM 1982 C C . VAL B 1 47 ? 13.399 8.740 35.430 1.00 23.75 ? 46 VAL B C 1 ATOM 1983 O O . VAL B 1 47 ? 13.220 9.678 36.218 1.00 20.99 ? 46 VAL B O 1 ATOM 1984 C CB . VAL B 1 47 ? 15.603 9.100 34.385 1.00 24.29 ? 46 VAL B CB 1 ATOM 1985 C CG1 . VAL B 1 47 ? 16.280 7.750 34.323 1.00 26.78 ? 46 VAL B CG1 1 ATOM 1986 C CG2 . VAL B 1 47 ? 16.274 10.099 33.510 1.00 24.08 ? 46 VAL B CG2 1 ATOM 1987 N N . HIS B 1 48 ? 13.094 7.490 35.717 1.00 23.98 ? 47 HIS B N 1 ATOM 1988 C CA . HIS B 1 48 ? 12.711 7.118 37.066 1.00 22.02 ? 47 HIS B CA 1 ATOM 1989 C C . HIS B 1 48 ? 13.678 6.070 37.568 1.00 24.52 ? 47 HIS B C 1 ATOM 1990 O O . HIS B 1 48 ? 13.951 5.089 36.868 1.00 27.02 ? 47 HIS B O 1 ATOM 1991 C CB . HIS B 1 48 ? 11.297 6.611 37.107 1.00 18.39 ? 47 HIS B CB 1 ATOM 1992 C CG . HIS B 1 48 ? 10.797 6.384 38.489 1.00 20.17 ? 47 HIS B CG 1 ATOM 1993 N ND1 . HIS B 1 48 ? 9.550 5.864 38.748 1.00 27.05 ? 47 HIS B ND1 1 ATOM 1994 C CD2 . HIS B 1 48 ? 11.374 6.594 39.692 1.00 26.76 ? 47 HIS B CD2 1 ATOM 1995 C CE1 . HIS B 1 48 ? 9.380 5.759 40.055 1.00 24.31 ? 47 HIS B CE1 1 ATOM 1996 N NE2 . HIS B 1 48 ? 10.470 6.202 40.651 1.00 23.65 ? 47 HIS B NE2 1 ATOM 1997 N N . HIS B 1 49 ? 14.224 6.294 38.756 1.00 24.45 ? 48 HIS B N 1 ATOM 1998 C CA . HIS B 1 49 ? 15.132 5.336 39.364 1.00 26.47 ? 48 HIS B CA 1 ATOM 1999 C C . HIS B 1 49 ? 14.630 5.042 40.771 1.00 29.41 ? 48 HIS B C 1 ATOM 2000 O O . HIS B 1 49 ? 14.250 5.968 41.506 1.00 27.31 ? 48 HIS B O 1 ATOM 2001 C CB . HIS B 1 49 ? 16.577 5.833 39.401 1.00 27.27 ? 48 HIS B CB 1 ATOM 2002 C CG . HIS B 1 49 ? 17.569 4.777 39.790 1.00 29.90 ? 48 HIS B CG 1 ATOM 2003 N ND1 . HIS B 1 49 ? 17.710 4.328 41.088 1.00 27.57 ? 48 HIS B ND1 1 ATOM 2004 C CD2 . HIS B 1 49 ? 18.480 4.095 39.052 1.00 24.10 ? 48 HIS B CD2 1 ATOM 2005 C CE1 . HIS B 1 49 ? 18.665 3.418 41.133 1.00 26.00 ? 48 HIS B CE1 1 ATOM 2006 N NE2 . HIS B 1 49 ? 19.150 3.263 39.912 1.00 26.69 ? 48 HIS B NE2 1 ATOM 2007 N N . PRO B 1 50 ? 14.597 3.779 41.173 1.00 32.12 ? 49 PRO B N 1 ATOM 2008 C CA . PRO B 1 50 ? 13.933 3.440 42.435 1.00 37.60 ? 49 PRO B CA 1 ATOM 2009 C C . PRO B 1 50 ? 14.595 4.075 43.652 1.00 38.21 ? 49 PRO B C 1 ATOM 2010 O O . PRO B 1 50 ? 13.904 4.375 44.634 1.00 39.75 ? 49 PRO B O 1 ATOM 2011 C CB . PRO B 1 50 ? 13.997 1.907 42.449 1.00 33.13 ? 49 PRO B CB 1 ATOM 2012 C CG . PRO B 1 50 ? 15.184 1.589 41.550 1.00 32.34 ? 49 PRO B CG 1 ATOM 2013 C CD . PRO B 1 50 ? 15.076 2.584 40.463 1.00 28.17 ? 49 PRO B CD 1 ATOM 2014 N N . GLN B 1 51 ? 15.901 4.328 43.613 1.00 34.14 ? 50 GLN B N 1 ATOM 2015 C CA . GLN B 1 51 ? 16.542 5.003 44.730 1.00 35.16 ? 50 GLN B CA 1 ATOM 2016 C C . GLN B 1 51 ? 16.765 6.491 44.493 1.00 39.95 ? 50 GLN B C 1 ATOM 2017 O O . GLN B 1 51 ? 16.701 7.271 45.445 1.00 44.90 ? 50 GLN B O 1 ATOM 2018 C CB . GLN B 1 51 ? 17.879 4.336 45.055 1.00 36.67 ? 50 GLN B CB 1 ATOM 2019 C CG . GLN B 1 51 ? 17.763 2.820 45.323 1.00 42.62 ? 50 GLN B CG 1 ATOM 2020 C CD . GLN B 1 51 ? 16.700 2.468 46.371 1.00 51.51 ? 50 GLN B CD 1 ATOM 2021 O OE1 . GLN B 1 51 ? 16.584 3.119 47.419 1.00 56.46 ? 50 GLN B OE1 1 ATOM 2022 N NE2 . GLN B 1 51 ? 15.914 1.438 46.084 1.00 43.85 ? 50 GLN B NE2 1 ATOM 2023 N N . TYR B 1 52 ? 16.988 6.909 43.252 1.00 37.03 ? 51 TYR B N 1 ATOM 2024 C CA . TYR B 1 52 ? 17.361 8.277 42.928 1.00 32.07 ? 51 TYR B CA 1 ATOM 2025 C C . TYR B 1 52 ? 16.200 9.145 42.445 1.00 34.20 ? 51 TYR B C 1 ATOM 2026 O O . TYR B 1 52 ? 16.429 10.296 42.092 1.00 38.32 ? 51 TYR B O 1 ATOM 2027 C CB . TYR B 1 52 ? 18.453 8.260 41.867 1.00 32.57 ? 51 TYR B CB 1 ATOM 2028 C CG . TYR B 1 52 ? 19.644 7.431 42.244 1.00 31.91 ? 51 TYR B CG 1 ATOM 2029 C CD1 . TYR B 1 52 ? 20.178 7.499 43.516 1.00 40.71 ? 51 TYR B CD1 1 ATOM 2030 C CD2 . TYR B 1 52 ? 20.245 6.577 41.322 1.00 43.43 ? 51 TYR B CD2 1 ATOM 2031 C CE1 . TYR B 1 52 ? 21.283 6.740 43.867 1.00 48.45 ? 51 TYR B CE1 1 ATOM 2032 C CE2 . TYR B 1 52 ? 21.354 5.802 41.661 1.00 37.92 ? 51 TYR B CE2 1 ATOM 2033 C CZ . TYR B 1 52 ? 21.865 5.898 42.937 1.00 42.66 ? 51 TYR B CZ 1 ATOM 2034 O OH . TYR B 1 52 ? 22.963 5.154 43.285 1.00 53.12 ? 51 TYR B OH 1 ATOM 2035 N N . GLY B 1 53 ? 14.975 8.635 42.406 1.00 30.47 ? 52 GLY B N 1 ATOM 2036 C CA . GLY B 1 53 ? 13.836 9.462 42.050 1.00 29.79 ? 52 GLY B CA 1 ATOM 2037 C C . GLY B 1 53 ? 13.766 9.850 40.577 1.00 27.60 ? 52 GLY B C 1 ATOM 2038 O O . GLY B 1 53 ? 14.511 9.372 39.734 1.00 28.26 ? 52 GLY B O 1 ATOM 2039 N N . PHE B 1 54 ? 12.844 10.762 40.289 1.00 26.79 ? 53 PHE B N 1 ATOM 2040 C CA . PHE B 1 54 ? 12.635 11.239 38.933 1.00 26.26 ? 53 PHE B CA 1 ATOM 2041 C C . PHE B 1 54 ? 13.717 12.223 38.523 1.00 25.92 ? 53 PHE B C 1 ATOM 2042 O O . PHE B 1 54 ? 14.356 12.866 39.350 1.00 33.61 ? 53 PHE B O 1 ATOM 2043 C CB . PHE B 1 54 ? 11.288 11.948 38.788 1.00 32.73 ? 53 PHE B CB 1 ATOM 2044 C CG . PHE B 1 54 ? 10.102 11.120 39.199 1.00 31.67 ? 53 PHE B CG 1 ATOM 2045 C CD1 . PHE B 1 54 ? 10.075 9.756 38.969 1.00 28.76 ? 53 PHE B CD1 1 ATOM 2046 C CD2 . PHE B 1 54 ? 9.004 11.722 39.825 1.00 30.22 ? 53 PHE B CD2 1 ATOM 2047 C CE1 . PHE B 1 54 ? 8.961 8.994 39.355 1.00 32.91 ? 53 PHE B CE1 1 ATOM 2048 C CE2 . PHE B 1 54 ? 7.902 10.986 40.204 1.00 31.94 ? 53 PHE B CE2 1 ATOM 2049 C CZ . PHE B 1 54 ? 7.886 9.604 39.974 1.00 34.39 ? 53 PHE B CZ 1 ATOM 2050 N N . SER B 1 55 ? 13.876 12.373 37.212 1.00 26.74 ? 54 SER B N 1 ATOM 2051 C CA . SER B 1 55 ? 14.669 13.446 36.630 1.00 23.94 ? 54 SER B CA 1 ATOM 2052 C C . SER B 1 55 ? 14.083 13.789 35.259 1.00 23.64 ? 54 SER B C 1 ATOM 2053 O O . SER B 1 55 ? 13.698 12.894 34.501 1.00 25.87 ? 54 SER B O 1 ATOM 2054 C CB . SER B 1 55 ? 16.145 13.033 36.538 1.00 28.73 ? 54 SER B CB 1 ATOM 2055 O OG . SER B 1 55 ? 16.924 13.899 35.724 1.00 24.96 ? 54 SER B OG 1 ATOM 2056 N N . VAL B 1 56 ? 13.965 15.082 34.964 1.00 23.68 ? 55 VAL B N 1 ATOM 2057 C CA . VAL B 1 56 ? 13.537 15.560 33.654 1.00 19.52 ? 55 VAL B CA 1 ATOM 2058 C C . VAL B 1 56 ? 14.667 16.389 33.067 1.00 24.88 ? 55 VAL B C 1 ATOM 2059 O O . VAL B 1 56 ? 15.321 17.139 33.795 1.00 34.51 ? 55 VAL B O 1 ATOM 2060 C CB . VAL B 1 56 ? 12.236 16.372 33.756 1.00 22.88 ? 55 VAL B CB 1 ATOM 2061 C CG1 . VAL B 1 56 ? 11.785 16.854 32.384 1.00 25.84 ? 55 VAL B CG1 1 ATOM 2062 C CG2 . VAL B 1 56 ? 11.152 15.535 34.421 1.00 18.67 ? 55 VAL B CG2 1 ATOM 2063 N N . GLN B 1 57 ? 14.926 16.238 31.767 1.00 26.29 ? 56 GLN B N 1 ATOM 2064 C CA . GLN B 1 57 ? 16.092 16.853 31.142 1.00 28.64 ? 56 GLN B CA 1 ATOM 2065 C C . GLN B 1 57 ? 15.713 17.853 30.059 1.00 23.68 ? 56 GLN B C 1 ATOM 2066 O O . GLN B 1 57 ? 14.596 17.859 29.537 1.00 28.16 ? 56 GLN B O 1 ATOM 2067 C CB . GLN B 1 57 ? 17.017 15.798 30.520 1.00 24.71 ? 56 GLN B CB 1 ATOM 2068 C CG . GLN B 1 57 ? 18.318 15.613 31.266 1.00 27.63 ? 56 GLN B CG 1 ATOM 2069 C CD . GLN B 1 57 ? 18.085 15.003 32.595 1.00 31.35 ? 56 GLN B CD 1 ATOM 2070 O OE1 . GLN B 1 57 ? 17.287 14.074 32.728 1.00 39.65 ? 56 GLN B OE1 1 ATOM 2071 N NE2 . GLN B 1 57 ? 18.765 15.517 33.606 1.00 33.74 ? 56 GLN B NE2 1 ATOM 2072 N N . GLY B 1 58 ? 16.684 18.685 29.708 1.00 24.86 ? 57 GLY B N 1 ATOM 2073 C CA . GLY B 1 58 ? 16.609 19.541 28.534 1.00 24.87 ? 57 GLY B CA 1 ATOM 2074 C C . GLY B 1 58 ? 15.493 20.564 28.617 1.00 32.99 ? 57 GLY B C 1 ATOM 2075 O O . GLY B 1 58 ? 15.120 21.052 29.694 1.00 35.22 ? 57 GLY B O 1 ATOM 2076 N N . ASP B 1 59 ? 14.942 20.895 27.454 1.00 34.32 ? 58 ASP B N 1 ATOM 2077 C CA . ASP B 1 59 ? 13.832 21.837 27.428 1.00 33.50 ? 58 ASP B CA 1 ATOM 2078 C C . ASP B 1 59 ? 12.521 21.199 27.886 1.00 27.53 ? 58 ASP B C 1 ATOM 2079 O O . ASP B 1 59 ? 11.471 21.834 27.772 1.00 30.22 ? 58 ASP B O 1 ATOM 2080 C CB . ASP B 1 59 ? 13.682 22.465 26.026 1.00 36.72 ? 58 ASP B CB 1 ATOM 2081 C CG . ASP B 1 59 ? 13.142 21.482 24.964 1.00 45.18 ? 58 ASP B CG 1 ATOM 2082 O OD1 . ASP B 1 59 ? 12.090 20.847 25.206 1.00 45.71 ? 58 ASP B OD1 1 ATOM 2083 O OD2 . ASP B 1 59 ? 13.732 21.380 23.859 1.00 42.85 ? 58 ASP B OD2 1 ATOM 2084 N N . TYR B 1 60 ? 12.551 19.969 28.402 1.00 24.10 ? 59 TYR B N 1 ATOM 2085 C CA . TYR B 1 60 ? 11.344 19.382 28.966 1.00 24.55 ? 59 TYR B CA 1 ATOM 2086 C C . TYR B 1 60 ? 11.123 19.777 30.414 1.00 25.01 ? 59 TYR B C 1 ATOM 2087 O O . TYR B 1 60 ? 10.007 19.600 30.928 1.00 27.15 ? 59 TYR B O 1 ATOM 2088 C CB . TYR B 1 60 ? 11.399 17.861 28.859 1.00 24.20 ? 59 TYR B CB 1 ATOM 2089 C CG . TYR B 1 60 ? 11.372 17.405 27.446 1.00 24.79 ? 59 TYR B CG 1 ATOM 2090 C CD1 . TYR B 1 60 ? 10.172 17.267 26.797 1.00 25.46 ? 59 TYR B CD1 1 ATOM 2091 C CD2 . TYR B 1 60 ? 12.545 17.145 26.741 1.00 26.59 ? 59 TYR B CD2 1 ATOM 2092 C CE1 . TYR B 1 60 ? 10.112 16.854 25.497 1.00 27.61 ? 59 TYR B CE1 1 ATOM 2093 C CE2 . TYR B 1 60 ? 12.496 16.738 25.412 1.00 26.48 ? 59 TYR B CE2 1 ATOM 2094 C CZ . TYR B 1 60 ? 11.257 16.586 24.806 1.00 27.12 ? 59 TYR B CZ 1 ATOM 2095 O OH . TYR B 1 60 ? 11.100 16.170 23.509 1.00 32.31 ? 59 TYR B OH 1 ATOM 2096 N N . GLN B 1 61 ? 12.149 20.299 31.083 1.00 22.54 ? 60 GLN B N 1 ATOM 2097 C CA . GLN B 1 61 ? 12.006 20.656 32.487 1.00 28.51 ? 60 GLN B CA 1 ATOM 2098 C C . GLN B 1 61 ? 10.915 21.700 32.669 1.00 33.05 ? 60 GLN B C 1 ATOM 2099 O O . GLN B 1 61 ? 10.797 22.645 31.879 1.00 32.53 ? 60 GLN B O 1 ATOM 2100 C CB . GLN B 1 61 ? 13.317 21.184 33.038 1.00 24.98 ? 60 GLN B CB 1 ATOM 2101 C CG . GLN B 1 61 ? 14.483 20.302 32.769 1.00 25.90 ? 60 GLN B CG 1 ATOM 2102 C CD . GLN B 1 61 ? 15.696 20.761 33.536 1.00 28.83 ? 60 GLN B CD 1 ATOM 2103 O OE1 . GLN B 1 61 ? 15.667 20.870 34.766 1.00 29.10 ? 60 GLN B OE1 1 ATOM 2104 N NE2 . GLN B 1 61 ? 16.761 21.064 32.820 1.00 29.64 ? 60 GLN B NE2 1 ATOM 2105 N N . GLY B 1 62 ? 10.113 21.525 33.725 1.00 28.27 ? 61 GLY B N 1 ATOM 2106 C CA . GLY B 1 62 ? 8.963 22.367 33.946 1.00 20.11 ? 61 GLY B CA 1 ATOM 2107 C C . GLY B 1 62 ? 7.745 22.011 33.129 1.00 23.74 ? 61 GLY B C 1 ATOM 2108 O O . GLY B 1 62 ? 6.673 22.549 33.404 1.00 30.42 ? 61 GLY B O 1 ATOM 2109 N N . ARG B 1 63 ? 7.859 21.092 32.162 1.00 28.88 ? 62 ARG B N 1 ATOM 2110 C CA . ARG B 1 63 ? 6.736 20.681 31.312 1.00 31.10 ? 62 ARG B CA 1 ATOM 2111 C C . ARG B 1 63 ? 6.404 19.188 31.350 1.00 28.37 ? 62 ARG B C 1 ATOM 2112 O O . ARG B 1 63 ? 5.549 18.752 30.579 1.00 27.32 ? 62 ARG B O 1 ATOM 2113 C CB . ARG B 1 63 ? 7.008 21.056 29.848 1.00 25.26 ? 62 ARG B CB 1 ATOM 2114 C CG . ARG B 1 63 ? 7.533 22.452 29.639 1.00 24.31 ? 62 ARG B CG 1 ATOM 2115 C CD . ARG B 1 63 ? 7.574 22.805 28.177 1.00 32.40 ? 62 ARG B CD 1 ATOM 2116 N NE . ARG B 1 63 ? 8.517 22.024 27.359 1.00 33.23 ? 62 ARG B NE 1 ATOM 2117 C CZ . ARG B 1 63 ? 8.160 21.258 26.324 1.00 30.99 ? 62 ARG B CZ 1 ATOM 2118 N NH1 . ARG B 1 63 ? 6.872 21.152 25.986 1.00 28.13 ? 62 ARG B NH1 1 ATOM 2119 N NH2 . ARG B 1 63 ? 9.081 20.606 25.617 1.00 22.08 ? 62 ARG B NH2 1 ATOM 2120 N N . VAL B 1 64 ? 7.048 18.389 32.198 1.00 24.62 ? 63 VAL B N 1 ATOM 2121 C CA . VAL B 1 64 ? 6.833 16.942 32.238 1.00 25.31 ? 63 VAL B CA 1 ATOM 2122 C C . VAL B 1 64 ? 6.434 16.526 33.646 1.00 23.26 ? 63 VAL B C 1 ATOM 2123 O O . VAL B 1 64 ? 7.128 16.846 34.616 1.00 25.54 ? 63 VAL B O 1 ATOM 2124 C CB . VAL B 1 64 ? 8.087 16.161 31.796 1.00 27.64 ? 63 VAL B CB 1 ATOM 2125 C CG1 . VAL B 1 64 ? 7.872 14.668 31.966 1.00 23.04 ? 63 VAL B CG1 1 ATOM 2126 C CG2 . VAL B 1 64 ? 8.440 16.479 30.348 1.00 24.73 ? 63 VAL B CG2 1 ATOM 2127 N N . LEU B 1 65 ? 5.345 15.782 33.752 1.00 24.38 ? 64 LEU B N 1 ATOM 2128 C CA . LEU B 1 65 ? 4.961 15.143 34.996 1.00 25.96 ? 64 LEU B CA 1 ATOM 2129 C C . LEU B 1 65 ? 4.991 13.626 34.847 1.00 28.27 ? 64 LEU B C 1 ATOM 2130 O O . LEU B 1 65 ? 4.497 13.087 33.853 1.00 33.87 ? 64 LEU B O 1 ATOM 2131 C CB . LEU B 1 65 ? 3.563 15.567 35.417 1.00 27.12 ? 64 LEU B CB 1 ATOM 2132 C CG . LEU B 1 65 ? 3.350 17.024 35.750 1.00 30.79 ? 64 LEU B CG 1 ATOM 2133 C CD1 . LEU B 1 65 ? 1.937 17.175 36.185 1.00 17.22 ? 64 LEU B CD1 1 ATOM 2134 C CD2 . LEU B 1 65 ? 4.328 17.452 36.844 1.00 34.18 ? 64 LEU B CD2 1 ATOM 2135 N N . PHE B 1 66 ? 5.563 12.937 35.836 1.00 29.30 ? 65 PHE B N 1 ATOM 2136 C CA . PHE B 1 66 ? 5.364 11.499 35.962 1.00 27.24 ? 65 PHE B CA 1 ATOM 2137 C C . PHE B 1 66 ? 3.997 11.256 36.583 1.00 30.68 ? 65 PHE B C 1 ATOM 2138 O O . PHE B 1 66 ? 3.651 11.880 37.589 1.00 33.64 ? 65 PHE B O 1 ATOM 2139 C CB . PHE B 1 66 ? 6.454 10.855 36.816 1.00 26.65 ? 65 PHE B CB 1 ATOM 2140 C CG . PHE B 1 66 ? 7.576 10.252 36.018 1.00 33.69 ? 65 PHE B CG 1 ATOM 2141 C CD1 . PHE B 1 66 ? 7.385 9.062 35.297 1.00 25.68 ? 65 PHE B CD1 1 ATOM 2142 C CD2 . PHE B 1 66 ? 8.832 10.865 35.997 1.00 33.40 ? 65 PHE B CD2 1 ATOM 2143 C CE1 . PHE B 1 66 ? 8.408 8.512 34.561 1.00 21.00 ? 65 PHE B CE1 1 ATOM 2144 C CE2 . PHE B 1 66 ? 9.875 10.321 35.261 1.00 29.12 ? 65 PHE B CE2 1 ATOM 2145 C CZ . PHE B 1 66 ? 9.663 9.134 34.536 1.00 27.43 ? 65 PHE B CZ 1 ATOM 2146 N N . LYS B 1 67 ? 3.215 10.366 35.968 1.00 28.54 ? 66 LYS B N 1 ATOM 2147 C CA . LYS B 1 67 ? 1.863 10.095 36.444 1.00 28.84 ? 66 LYS B CA 1 ATOM 2148 C C . LYS B 1 67 ? 1.871 9.615 37.893 1.00 39.04 ? 66 LYS B C 1 ATOM 2149 O O . LYS B 1 67 ? 1.111 10.121 38.737 1.00 34.61 ? 66 LYS B O 1 ATOM 2150 C CB . LYS B 1 67 ? 1.216 9.051 35.540 1.00 31.72 ? 66 LYS B CB 1 ATOM 2151 C CG . LYS B 1 67 ? -0.222 8.731 35.839 1.00 30.57 ? 66 LYS B CG 1 ATOM 2152 C CD . LYS B 1 67 ? -0.611 7.444 35.136 1.00 32.57 ? 66 LYS B CD 1 ATOM 2153 C CE . LYS B 1 67 ? -2.089 7.183 35.245 1.00 34.24 ? 66 LYS B CE 1 ATOM 2154 N NZ . LYS B 1 67 ? -2.780 8.274 34.547 1.00 34.72 ? 66 LYS B NZ 1 ATOM 2155 N N . ASN B 1 68 ? 2.719 8.629 38.199 1.00 32.59 ? 67 ASN B N 1 ATOM 2156 C CA . ASN B 1 68 ? 2.769 8.057 39.536 1.00 36.14 ? 67 ASN B CA 1 ATOM 2157 C C . ASN B 1 68 ? 4.114 7.380 39.744 1.00 35.10 ? 67 ASN B C 1 ATOM 2158 O O . ASN B 1 68 ? 4.920 7.250 38.821 1.00 37.83 ? 67 ASN B O 1 ATOM 2159 C CB . ASN B 1 68 ? 1.624 7.068 39.754 1.00 37.36 ? 67 ASN B CB 1 ATOM 2160 C CG . ASN B 1 68 ? 1.522 6.067 38.642 1.00 40.79 ? 67 ASN B CG 1 ATOM 2161 O OD1 . ASN B 1 68 ? 2.506 5.392 38.299 1.00 42.06 ? 67 ASN B OD1 1 ATOM 2162 N ND2 . ASN B 1 68 ? 0.339 5.988 38.029 1.00 36.12 ? 67 ASN B ND2 1 ATOM 2163 N N . TYR B 1 69 ? 4.322 6.915 40.973 1.00 31.51 ? 68 TYR B N 1 ATOM 2164 C CA . TYR B 1 69 ? 5.607 6.442 41.459 1.00 32.65 ? 68 TYR B CA 1 ATOM 2165 C C . TYR B 1 69 ? 5.907 4.982 41.136 1.00 40.55 ? 68 TYR B C 1 ATOM 2166 O O . TYR B 1 69 ? 7.026 4.531 41.391 1.00 42.30 ? 68 TYR B O 1 ATOM 2167 C CB . TYR B 1 69 ? 5.675 6.607 42.963 1.00 31.37 ? 68 TYR B CB 1 ATOM 2168 C CG . TYR B 1 69 ? 5.981 7.980 43.425 1.00 32.21 ? 68 TYR B CG 1 ATOM 2169 C CD1 . TYR B 1 69 ? 7.282 8.440 43.415 1.00 38.12 ? 68 TYR B CD1 1 ATOM 2170 C CD2 . TYR B 1 69 ? 4.990 8.808 43.919 1.00 32.86 ? 68 TYR B CD2 1 ATOM 2171 C CE1 . TYR B 1 69 ? 7.593 9.699 43.859 1.00 47.35 ? 68 TYR B CE1 1 ATOM 2172 C CE2 . TYR B 1 69 ? 5.292 10.080 44.378 1.00 35.95 ? 68 TYR B CE2 1 ATOM 2173 C CZ . TYR B 1 69 ? 6.600 10.519 44.352 1.00 34.41 ? 68 TYR B CZ 1 ATOM 2174 O OH . TYR B 1 69 ? 6.948 11.782 44.790 1.00 40.18 ? 68 TYR B OH 1 ATOM 2175 N N . SER B 1 70 ? 4.948 4.225 40.617 1.00 38.21 ? 69 SER B N 1 ATOM 2176 C CA . SER B 1 70 ? 5.204 2.827 40.315 1.00 24.54 ? 69 SER B CA 1 ATOM 2177 C C . SER B 1 70 ? 6.260 2.675 39.233 1.00 35.40 ? 69 SER B C 1 ATOM 2178 O O . SER B 1 70 ? 6.159 3.279 38.163 1.00 40.27 ? 69 SER B O 1 ATOM 2179 C CB . SER B 1 70 ? 3.919 2.154 39.862 1.00 33.27 ? 69 SER B CB 1 ATOM 2180 O OG . SER B 1 70 ? 4.188 0.816 39.497 1.00 41.11 ? 69 SER B OG 1 ATOM 2181 N N . LEU B 1 71 ? 7.255 1.820 39.492 1.00 37.28 ? 70 LEU B N 1 ATOM 2182 C CA . LEU B 1 71 ? 8.242 1.501 38.462 1.00 32.78 ? 70 LEU B CA 1 ATOM 2183 C C . LEU B 1 71 ? 7.649 0.784 37.253 1.00 31.29 ? 70 LEU B C 1 ATOM 2184 O O . LEU B 1 71 ? 8.288 0.760 36.204 1.00 31.74 ? 70 LEU B O 1 ATOM 2185 C CB . LEU B 1 71 ? 9.361 0.639 39.033 1.00 33.89 ? 70 LEU B CB 1 ATOM 2186 C CG . LEU B 1 71 ? 10.656 1.304 39.485 1.00 34.36 ? 70 LEU B CG 1 ATOM 2187 C CD1 . LEU B 1 71 ? 10.375 2.365 40.527 1.00 34.83 ? 70 LEU B CD1 1 ATOM 2188 C CD2 . LEU B 1 71 ? 11.556 0.214 40.033 1.00 34.71 ? 70 LEU B CD2 1 ATOM 2189 N N . ASN B 1 72 ? 6.461 0.197 37.362 1.00 34.19 ? 71 ASN B N 1 ATOM 2190 C CA . ASN B 1 72 ? 5.846 -0.489 36.230 1.00 37.30 ? 71 ASN B CA 1 ATOM 2191 C C . ASN B 1 72 ? 4.954 0.413 35.387 1.00 42.15 ? 71 ASN B C 1 ATOM 2192 O O . ASN B 1 72 ? 4.364 -0.059 34.408 1.00 38.04 ? 71 ASN B O 1 ATOM 2193 C CB . ASN B 1 72 ? 5.061 -1.701 36.727 1.00 34.33 ? 71 ASN B CB 1 ATOM 2194 C CG . ASN B 1 72 ? 5.968 -2.882 37.013 1.00 46.27 ? 71 ASN B CG 1 ATOM 2195 O OD1 . ASN B 1 72 ? 6.750 -2.872 37.970 1.00 47.39 ? 71 ASN B OD1 1 ATOM 2196 N ND2 . ASN B 1 72 ? 5.890 -3.900 36.167 1.00 49.37 ? 71 ASN B ND2 1 ATOM 2197 N N . ASP B 1 73 ? 4.879 1.702 35.725 1.00 40.73 ? 72 ASP B N 1 ATOM 2198 C CA . ASP B 1 73 ? 4.043 2.686 35.038 1.00 35.87 ? 72 ASP B CA 1 ATOM 2199 C C . ASP B 1 73 ? 4.944 3.866 34.674 1.00 34.42 ? 72 ASP B C 1 ATOM 2200 O O . ASP B 1 73 ? 5.223 4.742 35.503 1.00 35.60 ? 72 ASP B O 1 ATOM 2201 C CB . ASP B 1 73 ? 2.864 3.115 35.921 1.00 31.44 ? 72 ASP B CB 1 ATOM 2202 C CG . ASP B 1 73 ? 1.809 3.864 35.164 1.00 26.83 ? 72 ASP B CG 1 ATOM 2203 O OD1 . ASP B 1 73 ? 2.142 4.519 34.165 1.00 28.22 ? 72 ASP B OD1 1 ATOM 2204 O OD2 . ASP B 1 73 ? 0.635 3.793 35.565 1.00 38.90 ? 72 ASP B OD2 1 ATOM 2205 N N . ALA B 1 74 ? 5.404 3.882 33.436 1.00 30.07 ? 73 ALA B N 1 ATOM 2206 C CA . ALA B 1 74 ? 6.291 4.917 32.940 1.00 26.10 ? 73 ALA B CA 1 ATOM 2207 C C . ALA B 1 74 ? 5.544 6.079 32.297 1.00 25.28 ? 73 ALA B C 1 ATOM 2208 O O . ALA B 1 74 ? 6.173 6.895 31.619 1.00 27.81 ? 73 ALA B O 1 ATOM 2209 C CB . ALA B 1 74 ? 7.262 4.315 31.931 1.00 19.73 ? 73 ALA B CB 1 ATOM 2210 N N . THR B 1 75 ? 4.228 6.161 32.468 1.00 22.23 ? 74 THR B N 1 ATOM 2211 C CA . THR B 1 75 ? 3.446 7.193 31.794 1.00 22.61 ? 74 THR B CA 1 ATOM 2212 C C . THR B 1 75 ? 3.873 8.576 32.266 1.00 22.76 ? 74 THR B C 1 ATOM 2213 O O . THR B 1 75 ? 4.004 8.825 33.471 1.00 21.62 ? 74 THR B O 1 ATOM 2214 C CB . THR B 1 75 ? 1.946 6.978 32.073 1.00 29.95 ? 74 THR B CB 1 ATOM 2215 O OG1 . THR B 1 75 ? 1.523 5.705 31.559 1.00 29.59 ? 74 THR B OG1 1 ATOM 2216 C CG2 . THR B 1 75 ? 1.079 8.098 31.477 1.00 19.99 ? 74 THR B CG2 1 ATOM 2217 N N . ILE B 1 76 ? 4.078 9.485 31.317 1.00 21.23 ? 75 ILE B N 1 ATOM 2218 C CA . ILE B 1 76 ? 4.280 10.893 31.633 1.00 23.98 ? 75 ILE B CA 1 ATOM 2219 C C . ILE B 1 76 ? 3.272 11.718 30.850 1.00 25.68 ? 75 ILE B C 1 ATOM 2220 O O . ILE B 1 76 ? 2.668 11.255 29.879 1.00 24.74 ? 75 ILE B O 1 ATOM 2221 C CB . ILE B 1 76 ? 5.706 11.386 31.309 1.00 23.86 ? 75 ILE B CB 1 ATOM 2222 C CG1 . ILE B 1 76 ? 5.946 11.253 29.801 1.00 28.82 ? 75 ILE B CG1 1 ATOM 2223 C CG2 . ILE B 1 76 ? 6.746 10.610 32.109 1.00 21.98 ? 75 ILE B CG2 1 ATOM 2224 C CD1 . ILE B 1 76 ? 7.230 11.874 29.296 1.00 17.01 ? 75 ILE B CD1 1 ATOM 2225 N N . THR B 1 77 ? 3.091 12.961 31.294 1.00 29.01 ? 76 THR B N 1 ATOM 2226 C CA . THR B 1 77 ? 2.334 13.949 30.544 1.00 24.47 ? 76 THR B CA 1 ATOM 2227 C C . THR B 1 77 ? 3.241 15.123 30.218 1.00 28.07 ? 76 THR B C 1 ATOM 2228 O O . THR B 1 77 ? 4.022 15.586 31.063 1.00 23.06 ? 76 THR B O 1 ATOM 2229 C CB . THR B 1 77 ? 1.070 14.436 31.284 1.00 28.00 ? 76 THR B CB 1 ATOM 2230 O OG1 . THR B 1 77 ? 1.408 14.970 32.563 1.00 33.90 ? 76 THR B OG1 1 ATOM 2231 C CG2 . THR B 1 77 ? 0.122 13.295 31.496 1.00 21.36 ? 76 THR B CG2 1 ATOM 2232 N N . LEU B 1 78 ? 3.134 15.571 28.972 1.00 28.50 ? 77 LEU B N 1 ATOM 2233 C CA . LEU B 1 78 ? 3.918 16.662 28.426 1.00 31.60 ? 77 LEU B CA 1 ATOM 2234 C C . LEU B 1 78 ? 3.007 17.874 28.258 1.00 30.11 ? 77 LEU B C 1 ATOM 2235 O O . LEU B 1 78 ? 1.841 17.735 27.868 1.00 31.26 ? 77 LEU B O 1 ATOM 2236 C CB . LEU B 1 78 ? 4.546 16.234 27.093 1.00 26.01 ? 77 LEU B CB 1 ATOM 2237 C CG . LEU B 1 78 ? 5.533 17.146 26.378 1.00 31.22 ? 77 LEU B CG 1 ATOM 2238 C CD1 . LEU B 1 78 ? 6.659 17.583 27.297 1.00 27.72 ? 77 LEU B CD1 1 ATOM 2239 C CD2 . LEU B 1 78 ? 6.090 16.390 25.183 1.00 29.48 ? 77 LEU B CD2 1 ATOM 2240 N N . HIS B 1 79 ? 3.542 19.055 28.563 1.00 26.64 ? 78 HIS B N 1 ATOM 2241 C CA . HIS B 1 79 ? 2.768 20.281 28.653 1.00 29.14 ? 78 HIS B CA 1 ATOM 2242 C C . HIS B 1 79 ? 3.458 21.393 27.877 1.00 27.56 ? 78 HIS B C 1 ATOM 2243 O O . HIS B 1 79 ? 4.645 21.305 27.555 1.00 24.82 ? 78 HIS B O 1 ATOM 2244 C CB . HIS B 1 79 ? 2.572 20.695 30.113 1.00 24.15 ? 78 HIS B CB 1 ATOM 2245 C CG . HIS B 1 79 ? 1.971 19.621 30.953 1.00 27.37 ? 78 HIS B CG 1 ATOM 2246 N ND1 . HIS B 1 79 ? 0.675 19.679 31.415 1.00 28.18 ? 78 HIS B ND1 1 ATOM 2247 C CD2 . HIS B 1 79 ? 2.475 18.435 31.380 1.00 26.01 ? 78 HIS B CD2 1 ATOM 2248 C CE1 . HIS B 1 79 ? 0.410 18.586 32.115 1.00 24.16 ? 78 HIS B CE1 1 ATOM 2249 N NE2 . HIS B 1 79 ? 1.484 17.814 32.105 1.00 27.43 ? 78 HIS B NE2 1 ATOM 2250 N N . ASN B 1 80 ? 2.686 22.445 27.580 1.00 30.68 ? 79 ASN B N 1 ATOM 2251 C CA . ASN B 1 80 ? 3.145 23.575 26.771 1.00 25.04 ? 79 ASN B CA 1 ATOM 2252 C C . ASN B 1 80 ? 3.799 23.087 25.480 1.00 27.07 ? 79 ASN B C 1 ATOM 2253 O O . ASN B 1 80 ? 4.916 23.474 25.139 1.00 33.06 ? 79 ASN B O 1 ATOM 2254 C CB . ASN B 1 80 ? 4.114 24.456 27.558 1.00 42.30 ? 79 ASN B CB 1 ATOM 2255 C CG . ASN B 1 80 ? 3.449 25.207 28.699 1.00 47.45 ? 79 ASN B CG 1 ATOM 2256 O OD1 . ASN B 1 80 ? 2.271 25.000 28.998 1.00 51.44 ? 79 ASN B OD1 1 ATOM 2257 N ND2 . ASN B 1 80 ? 4.217 26.078 29.358 1.00 46.81 ? 79 ASN B ND2 1 ATOM 2258 N N . ILE B 1 81 ? 3.088 22.204 24.774 1.00 27.32 ? 80 ILE B N 1 ATOM 2259 C CA . ILE B 1 81 ? 3.621 21.548 23.591 1.00 20.40 ? 80 ILE B CA 1 ATOM 2260 C C . ILE B 1 81 ? 4.043 22.549 22.531 1.00 23.25 ? 80 ILE B C 1 ATOM 2261 O O . ILE B 1 81 ? 3.319 23.506 22.233 1.00 26.52 ? 80 ILE B O 1 ATOM 2262 C CB . ILE B 1 81 ? 2.560 20.598 23.026 1.00 23.24 ? 80 ILE B CB 1 ATOM 2263 C CG1 . ILE B 1 81 ? 2.518 19.323 23.861 1.00 32.27 ? 80 ILE B CG1 1 ATOM 2264 C CG2 . ILE B 1 81 ? 2.840 20.336 21.552 1.00 19.36 ? 80 ILE B CG2 1 ATOM 2265 C CD1 . ILE B 1 81 ? 1.252 18.532 23.682 1.00 38.27 ? 80 ILE B CD1 1 ATOM 2266 N N . GLY B 1 82 ? 5.218 22.311 21.933 1.00 22.86 ? 81 GLY B N 1 ATOM 2267 C CA . GLY B 1 82 ? 5.705 23.106 20.823 1.00 17.35 ? 81 GLY B CA 1 ATOM 2268 C C . GLY B 1 82 ? 6.146 22.225 19.664 1.00 20.04 ? 81 GLY B C 1 ATOM 2269 O O . GLY B 1 82 ? 6.064 20.995 19.723 1.00 16.70 ? 81 GLY B O 1 ATOM 2270 N N . PHE B 1 83 ? 6.610 22.888 18.602 1.00 22.71 ? 82 PHE B N 1 ATOM 2271 C CA . PHE B 1 83 ? 6.925 22.148 17.380 1.00 26.40 ? 82 PHE B CA 1 ATOM 2272 C C . PHE B 1 83 ? 8.021 21.126 17.628 1.00 24.35 ? 82 PHE B C 1 ATOM 2273 O O . PHE B 1 83 ? 7.972 20.014 17.093 1.00 34.31 ? 82 PHE B O 1 ATOM 2274 C CB . PHE B 1 83 ? 7.335 23.097 16.253 1.00 22.60 ? 82 PHE B CB 1 ATOM 2275 C CG . PHE B 1 83 ? 6.211 23.928 15.717 1.00 21.79 ? 82 PHE B CG 1 ATOM 2276 C CD1 . PHE B 1 83 ? 5.107 23.323 15.105 1.00 20.50 ? 82 PHE B CD1 1 ATOM 2277 C CD2 . PHE B 1 83 ? 6.263 25.317 15.783 1.00 21.91 ? 82 PHE B CD2 1 ATOM 2278 C CE1 . PHE B 1 83 ? 4.057 24.103 14.586 1.00 21.17 ? 82 PHE B CE1 1 ATOM 2279 C CE2 . PHE B 1 83 ? 5.209 26.110 15.283 1.00 22.04 ? 82 PHE B CE2 1 ATOM 2280 C CZ . PHE B 1 83 ? 4.109 25.496 14.683 1.00 25.32 ? 82 PHE B CZ 1 ATOM 2281 N N . SER B 1 84 ? 9.007 21.471 18.459 1.00 25.48 ? 83 SER B N 1 ATOM 2282 C CA . SER B 1 84 ? 10.127 20.563 18.686 1.00 23.28 ? 83 SER B CA 1 ATOM 2283 C C . SER B 1 84 ? 9.716 19.299 19.419 1.00 23.64 ? 83 SER B C 1 ATOM 2284 O O . SER B 1 84 ? 10.477 18.325 19.406 1.00 31.68 ? 83 SER B O 1 ATOM 2285 C CB . SER B 1 84 ? 11.218 21.251 19.483 1.00 21.48 ? 83 SER B CB 1 ATOM 2286 O OG . SER B 1 84 ? 10.818 21.367 20.831 1.00 25.31 ? 83 SER B OG 1 ATOM 2287 N N . ASP B 1 85 ? 8.538 19.282 20.050 1.00 20.89 ? 84 ASP B N 1 ATOM 2288 C CA . ASP B 1 85 ? 8.079 18.060 20.705 1.00 22.69 ? 84 ASP B CA 1 ATOM 2289 C C . ASP B 1 85 ? 7.640 16.982 19.724 1.00 24.33 ? 84 ASP B C 1 ATOM 2290 O O . ASP B 1 85 ? 7.358 15.862 20.159 1.00 26.06 ? 84 ASP B O 1 ATOM 2291 C CB . ASP B 1 85 ? 6.939 18.361 21.676 1.00 18.17 ? 84 ASP B CB 1 ATOM 2292 C CG . ASP B 1 85 ? 7.394 19.157 22.877 1.00 26.54 ? 84 ASP B CG 1 ATOM 2293 O OD1 . ASP B 1 85 ? 8.562 19.014 23.296 1.00 35.13 ? 84 ASP B OD1 1 ATOM 2294 O OD2 . ASP B 1 85 ? 6.598 19.946 23.401 1.00 30.96 ? 84 ASP B OD2 1 ATOM 2295 N N . SER B 1 86 ? 7.586 17.263 18.425 1.00 24.83 ? 85 SER B N 1 ATOM 2296 C CA . SER B 1 86 ? 7.271 16.194 17.481 1.00 28.72 ? 85 SER B CA 1 ATOM 2297 C C . SER B 1 86 ? 8.473 15.271 17.295 1.00 27.64 ? 85 SER B C 1 ATOM 2298 O O . SER B 1 86 ? 9.628 15.673 17.447 1.00 33.30 ? 85 SER B O 1 ATOM 2299 C CB . SER B 1 86 ? 6.827 16.757 16.127 1.00 21.74 ? 85 SER B CB 1 ATOM 2300 O OG . SER B 1 86 ? 7.906 17.364 15.428 1.00 31.47 ? 85 SER B OG 1 ATOM 2301 N N . GLY B 1 87 ? 8.193 14.025 16.986 1.00 21.98 ? 86 GLY B N 1 ATOM 2302 C CA . GLY B 1 87 ? 9.245 13.099 16.669 1.00 23.29 ? 86 GLY B CA 1 ATOM 2303 C C . GLY B 1 87 ? 8.984 11.772 17.315 1.00 25.94 ? 86 GLY B C 1 ATOM 2304 O O . GLY B 1 87 ? 7.886 11.503 17.795 1.00 24.89 ? 86 GLY B O 1 ATOM 2305 N N . LYS B 1 88 ? 10.027 10.947 17.335 1.00 30.55 ? 87 LYS B N 1 ATOM 2306 C CA . LYS B 1 88 ? 9.941 9.584 17.837 1.00 29.68 ? 87 LYS B CA 1 ATOM 2307 C C . LYS B 1 88 ? 10.528 9.503 19.242 1.00 31.14 ? 87 LYS B C 1 ATOM 2308 O O . LYS B 1 88 ? 11.675 9.895 19.468 1.00 36.70 ? 87 LYS B O 1 ATOM 2309 C CB . LYS B 1 88 ? 10.657 8.612 16.896 1.00 31.89 ? 87 LYS B CB 1 ATOM 2310 C CG . LYS B 1 88 ? 10.491 7.142 17.299 1.00 37.87 ? 87 LYS B CG 1 ATOM 2311 C CD . LYS B 1 88 ? 11.030 6.196 16.252 1.00 45.50 ? 87 LYS B CD 1 ATOM 2312 C CE . LYS B 1 88 ? 10.066 6.067 15.091 1.00 58.39 ? 87 LYS B CE 1 ATOM 2313 N NZ . LYS B 1 88 ? 10.472 4.975 14.171 1.00 63.47 ? 87 LYS B NZ 1 ATOM 2314 N N . TYR B 1 89 ? 9.734 8.992 20.173 1.00 27.92 ? 88 TYR B N 1 ATOM 2315 C CA . TYR B 1 89 ? 10.126 8.780 21.552 1.00 26.95 ? 88 TYR B CA 1 ATOM 2316 C C . TYR B 1 89 ? 10.318 7.289 21.786 1.00 33.47 ? 88 TYR B C 1 ATOM 2317 O O . TYR B 1 89 ? 9.717 6.464 21.097 1.00 33.86 ? 88 TYR B O 1 ATOM 2318 C CB . TYR B 1 89 ? 9.071 9.324 22.514 1.00 19.69 ? 88 TYR B CB 1 ATOM 2319 C CG . TYR B 1 89 ? 8.925 10.818 22.436 1.00 28.93 ? 88 TYR B CG 1 ATOM 2320 C CD1 . TYR B 1 89 ? 8.246 11.419 21.385 1.00 24.46 ? 88 TYR B CD1 1 ATOM 2321 C CD2 . TYR B 1 89 ? 9.468 11.639 23.417 1.00 35.61 ? 88 TYR B CD2 1 ATOM 2322 C CE1 . TYR B 1 89 ? 8.123 12.780 21.302 1.00 24.96 ? 88 TYR B CE1 1 ATOM 2323 C CE2 . TYR B 1 89 ? 9.346 13.016 23.350 1.00 32.46 ? 88 TYR B CE2 1 ATOM 2324 C CZ . TYR B 1 89 ? 8.675 13.581 22.287 1.00 31.74 ? 88 TYR B CZ 1 ATOM 2325 O OH . TYR B 1 89 ? 8.555 14.948 22.210 1.00 28.34 ? 88 TYR B OH 1 ATOM 2326 N N . ILE B 1 90 ? 11.140 6.957 22.781 1.00 26.98 ? 89 ILE B N 1 ATOM 2327 C CA . ILE B 1 90 ? 11.389 5.583 23.197 1.00 28.21 ? 89 ILE B CA 1 ATOM 2328 C C . ILE B 1 90 ? 11.069 5.466 24.678 1.00 26.16 ? 89 ILE B C 1 ATOM 2329 O O . ILE B 1 90 ? 11.665 6.171 25.496 1.00 26.56 ? 89 ILE B O 1 ATOM 2330 C CB . ILE B 1 90 ? 12.843 5.173 22.935 1.00 34.20 ? 89 ILE B CB 1 ATOM 2331 C CG1 . ILE B 1 90 ? 13.128 5.235 21.449 1.00 32.58 ? 89 ILE B CG1 1 ATOM 2332 C CG2 . ILE B 1 90 ? 13.117 3.776 23.440 1.00 33.24 ? 89 ILE B CG2 1 ATOM 2333 C CD1 . ILE B 1 90 ? 12.432 4.195 20.692 1.00 39.75 ? 89 ILE B CD1 1 ATOM 2334 N N . CYS B 1 91 ? 10.144 4.575 25.028 1.00 29.67 ? 90 CYS B N 1 ATOM 2335 C CA . CYS B 1 91 ? 10.005 4.139 26.414 1.00 27.79 ? 90 CYS B CA 1 ATOM 2336 C C . CYS B 1 91 ? 10.941 2.962 26.676 1.00 28.58 ? 90 CYS B C 1 ATOM 2337 O O . CYS B 1 91 ? 10.929 1.968 25.942 1.00 31.83 ? 90 CYS B O 1 ATOM 2338 C CB . CYS B 1 91 ? 8.573 3.739 26.742 1.00 19.57 ? 90 CYS B CB 1 ATOM 2339 S SG . CYS B 1 91 ? 8.342 3.481 28.525 1.00 25.47 ? 90 CYS B SG 1 ATOM 2340 N N . LYS B 1 92 ? 11.739 3.062 27.727 1.00 24.51 ? 91 LYS B N 1 ATOM 2341 C CA . LYS B 1 92 ? 12.786 2.079 27.960 1.00 31.45 ? 91 LYS B CA 1 ATOM 2342 C C . LYS B 1 92 ? 12.710 1.591 29.403 1.00 33.65 ? 91 LYS B C 1 ATOM 2343 O O . LYS B 1 92 ? 12.560 2.394 30.334 1.00 28.15 ? 91 LYS B O 1 ATOM 2344 C CB . LYS B 1 92 ? 14.139 2.695 27.627 1.00 29.13 ? 91 LYS B CB 1 ATOM 2345 C CG . LYS B 1 92 ? 15.259 1.730 27.406 1.00 41.64 ? 91 LYS B CG 1 ATOM 2346 C CD . LYS B 1 92 ? 16.512 2.525 27.073 1.00 42.31 ? 91 LYS B CD 1 ATOM 2347 C CE . LYS B 1 92 ? 17.656 1.644 26.626 1.00 56.84 ? 91 LYS B CE 1 ATOM 2348 N NZ . LYS B 1 92 ? 18.850 2.472 26.232 1.00 53.90 ? 91 LYS B NZ 1 ATOM 2349 N N . ALA B 1 93 ? 12.724 0.268 29.575 1.00 38.36 ? 92 ALA B N 1 ATOM 2350 C CA . ALA B 1 93 ? 12.863 -0.382 30.879 1.00 36.07 ? 92 ALA B CA 1 ATOM 2351 C C . ALA B 1 93 ? 14.223 -1.065 30.899 1.00 33.48 ? 92 ALA B C 1 ATOM 2352 O O . ALA B 1 93 ? 14.492 -1.948 30.077 1.00 31.93 ? 92 ALA B O 1 ATOM 2353 C CB . ALA B 1 93 ? 11.747 -1.396 31.132 1.00 33.85 ? 92 ALA B CB 1 ATOM 2354 N N . VAL B 1 94 ? 15.093 -0.641 31.795 1.00 34.31 ? 93 VAL B N 1 ATOM 2355 C CA . VAL B 1 94 ? 16.302 -1.406 32.075 1.00 39.61 ? 93 VAL B CA 1 ATOM 2356 C C . VAL B 1 94 ? 16.015 -2.334 33.243 1.00 34.93 ? 93 VAL B C 1 ATOM 2357 O O . VAL B 1 94 ? 15.443 -1.931 34.266 1.00 32.64 ? 93 VAL B O 1 ATOM 2358 C CB . VAL B 1 94 ? 17.504 -0.496 32.362 1.00 34.53 ? 93 VAL B CB 1 ATOM 2359 C CG1 . VAL B 1 94 ? 18.743 -1.341 32.631 1.00 28.92 ? 93 VAL B CG1 1 ATOM 2360 C CG2 . VAL B 1 94 ? 17.731 0.443 31.189 1.00 34.24 ? 93 VAL B CG2 1 ATOM 2361 N N . THR B 1 95 ? 16.390 -3.588 33.082 1.00 37.15 ? 94 THR B N 1 ATOM 2362 C CA . THR B 1 95 ? 16.004 -4.610 34.029 1.00 39.25 ? 94 THR B CA 1 ATOM 2363 C C . THR B 1 95 ? 17.232 -5.375 34.487 1.00 33.23 ? 94 THR B C 1 ATOM 2364 O O . THR B 1 95 ? 18.285 -5.343 33.839 1.00 32.21 ? 94 THR B O 1 ATOM 2365 C CB . THR B 1 95 ? 14.969 -5.536 33.397 1.00 38.20 ? 94 THR B CB 1 ATOM 2366 O OG1 . THR B 1 95 ? 15.463 -6.044 32.145 1.00 32.22 ? 94 THR B OG1 1 ATOM 2367 C CG2 . THR B 1 95 ? 13.648 -4.785 33.168 1.00 36.27 ? 94 THR B CG2 1 ATOM 2368 N N . PHE B 1 96 ? 17.083 -6.038 35.627 1.00 27.57 ? 95 PHE B N 1 ATOM 2369 C CA . PHE B 1 96 ? 18.116 -6.890 36.166 1.00 29.55 ? 95 PHE B CA 1 ATOM 2370 C C . PHE B 1 96 ? 17.654 -8.333 36.273 1.00 27.14 ? 95 PHE B C 1 ATOM 2371 O O . PHE B 1 96 ? 16.673 -8.586 36.934 1.00 38.92 ? 95 PHE B O 1 ATOM 2372 C CB . PHE B 1 96 ? 18.540 -6.408 37.550 1.00 27.47 ? 95 PHE B CB 1 ATOM 2373 C CG . PHE B 1 96 ? 19.620 -7.262 38.180 1.00 30.20 ? 95 PHE B CG 1 ATOM 2374 C CD1 . PHE B 1 96 ? 20.973 -6.996 37.934 1.00 27.72 ? 95 PHE B CD1 1 ATOM 2375 C CD2 . PHE B 1 96 ? 19.284 -8.348 38.986 1.00 21.95 ? 95 PHE B CD2 1 ATOM 2376 C CE1 . PHE B 1 96 ? 21.992 -7.781 38.518 1.00 25.71 ? 95 PHE B CE1 1 ATOM 2377 C CE2 . PHE B 1 96 ? 20.259 -9.128 39.579 1.00 24.10 ? 95 PHE B CE2 1 ATOM 2378 C CZ . PHE B 1 96 ? 21.635 -8.854 39.345 1.00 32.01 ? 95 PHE B CZ 1 ATOM 2379 N N . PRO B 1 97 ? 18.413 -9.298 35.727 1.00 30.63 ? 96 PRO B N 1 ATOM 2380 C CA . PRO B 1 97 ? 19.700 -9.241 34.994 1.00 34.18 ? 96 PRO B CA 1 ATOM 2381 C C . PRO B 1 97 ? 19.709 -9.084 33.457 1.00 30.63 ? 96 PRO B C 1 ATOM 2382 O O . PRO B 1 97 ? 20.793 -8.979 32.885 1.00 34.93 ? 96 PRO B O 1 ATOM 2383 C CB . PRO B 1 97 ? 20.327 -10.606 35.341 1.00 29.78 ? 96 PRO B CB 1 ATOM 2384 C CG . PRO B 1 97 ? 19.117 -11.523 35.490 1.00 21.20 ? 96 PRO B CG 1 ATOM 2385 C CD . PRO B 1 97 ? 18.161 -10.660 36.268 1.00 27.83 ? 96 PRO B CD 1 ATOM 2386 N N . LEU B 1 98 ? 18.558 -9.094 32.785 1.00 34.37 ? 97 LEU B N 1 ATOM 2387 C CA . LEU B 1 98 ? 18.580 -9.276 31.337 1.00 29.68 ? 97 LEU B CA 1 ATOM 2388 C C . LEU B 1 98 ? 18.864 -7.990 30.585 1.00 41.25 ? 97 LEU B C 1 ATOM 2389 O O . LEU B 1 98 ? 19.182 -8.049 29.394 1.00 45.72 ? 97 LEU B O 1 ATOM 2390 C CB . LEU B 1 98 ? 17.256 -9.868 30.832 1.00 44.98 ? 97 LEU B CB 1 ATOM 2391 C CG . LEU B 1 98 ? 16.759 -11.273 31.243 1.00 45.48 ? 97 LEU B CG 1 ATOM 2392 C CD1 . LEU B 1 98 ? 15.556 -11.692 30.431 1.00 52.16 ? 97 LEU B CD1 1 ATOM 2393 C CD2 . LEU B 1 98 ? 17.848 -12.330 31.212 1.00 37.69 ? 97 LEU B CD2 1 ATOM 2394 N N . GLY B 1 99 ? 18.752 -6.838 31.238 1.00 44.20 ? 98 GLY B N 1 ATOM 2395 C CA . GLY B 1 99 ? 19.007 -5.568 30.579 1.00 42.10 ? 98 GLY B CA 1 ATOM 2396 C C . GLY B 1 99 ? 17.800 -4.836 30.004 1.00 38.70 ? 98 GLY B C 1 ATOM 2397 O O . GLY B 1 99 ? 16.688 -4.896 30.531 1.00 37.58 ? 98 GLY B O 1 ATOM 2398 N N . ASN B 1 100 ? 18.009 -4.159 28.891 1.00 35.67 ? 99 ASN B N 1 ATOM 2399 C CA . ASN B 1 100 ? 17.049 -3.183 28.420 1.00 48.01 ? 99 ASN B CA 1 ATOM 2400 C C . ASN B 1 100 ? 15.993 -3.795 27.509 1.00 56.35 ? 99 ASN B C 1 ATOM 2401 O O . ASN B 1 100 ? 16.214 -4.811 26.845 1.00 53.44 ? 99 ASN B O 1 ATOM 2402 C CB . ASN B 1 100 ? 17.759 -2.057 27.685 1.00 46.90 ? 99 ASN B CB 1 ATOM 2403 C CG . ASN B 1 100 ? 18.538 -2.555 26.521 1.00 58.45 ? 99 ASN B CG 1 ATOM 2404 O OD1 . ASN B 1 100 ? 19.130 -3.635 26.581 1.00 68.94 ? 99 ASN B OD1 1 ATOM 2405 N ND2 . ASN B 1 100 ? 18.547 -1.785 25.438 1.00 69.29 ? 99 ASN B ND2 1 ATOM 2406 N N . ALA B 1 101 ? 14.825 -3.157 27.509 1.00 48.20 ? 100 ALA B N 1 ATOM 2407 C CA . ALA B 1 101 ? 13.738 -3.440 26.591 1.00 40.45 ? 100 ALA B CA 1 ATOM 2408 C C . ALA B 1 101 ? 13.084 -2.101 26.283 1.00 43.45 ? 100 ALA B C 1 ATOM 2409 O O . ALA B 1 101 ? 13.218 -1.145 27.051 1.00 40.65 ? 100 ALA B O 1 ATOM 2410 C CB . ALA B 1 101 ? 12.738 -4.440 27.187 1.00 34.00 ? 100 ALA B CB 1 ATOM 2411 N N . GLN B 1 102 ? 12.387 -2.018 25.151 1.00 37.80 ? 101 GLN B N 1 ATOM 2412 C CA . GLN B 1 102 ? 11.870 -0.720 24.752 1.00 37.70 ? 101 GLN B CA 1 ATOM 2413 C C . GLN B 1 102 ? 10.713 -0.860 23.767 1.00 38.27 ? 101 GLN B C 1 ATOM 2414 O O . GLN B 1 102 ? 10.486 -1.921 23.185 1.00 33.15 ? 101 GLN B O 1 ATOM 2415 C CB . GLN B 1 102 ? 12.986 0.128 24.163 1.00 24.58 ? 101 GLN B CB 1 ATOM 2416 C CG . GLN B 1 102 ? 13.411 -0.281 22.790 1.00 32.21 ? 101 GLN B CG 1 ATOM 2417 C CD . GLN B 1 102 ? 14.596 0.533 22.311 1.00 33.62 ? 101 GLN B CD 1 ATOM 2418 O OE1 . GLN B 1 102 ? 14.614 1.032 21.185 1.00 40.65 ? 101 GLN B OE1 1 ATOM 2419 N NE2 . GLN B 1 102 ? 15.602 0.661 23.166 1.00 33.08 ? 101 GLN B NE2 1 ATOM 2420 N N . SER B 1 103 ? 9.979 0.247 23.601 1.00 31.06 ? 102 SER B N 1 ATOM 2421 C CA . SER B 1 103 ? 8.994 0.431 22.540 1.00 32.76 ? 102 SER B CA 1 ATOM 2422 C C . SER B 1 103 ? 8.869 1.919 22.232 1.00 34.46 ? 102 SER B C 1 ATOM 2423 O O . SER B 1 103 ? 9.048 2.765 23.112 1.00 29.26 ? 102 SER B O 1 ATOM 2424 C CB . SER B 1 103 ? 7.620 -0.132 22.910 1.00 29.48 ? 102 SER B CB 1 ATOM 2425 O OG . SER B 1 103 ? 7.695 -1.528 23.095 1.00 40.03 ? 102 SER B OG 1 ATOM 2426 N N . SER B 1 104 ? 8.538 2.228 20.979 1.00 33.47 ? 103 SER B N 1 ATOM 2427 C CA . SER B 1 104 ? 8.569 3.589 20.460 1.00 33.53 ? 103 SER B CA 1 ATOM 2428 C C . SER B 1 104 ? 7.161 4.161 20.301 1.00 36.73 ? 103 SER B C 1 ATOM 2429 O O . SER B 1 104 ? 6.203 3.427 20.053 1.00 35.81 ? 103 SER B O 1 ATOM 2430 C CB . SER B 1 104 ? 9.288 3.638 19.110 1.00 32.53 ? 103 SER B CB 1 ATOM 2431 O OG . SER B 1 104 ? 8.581 2.884 18.151 1.00 35.99 ? 103 SER B OG 1 ATOM 2432 N N . THR B 1 105 ? 7.056 5.490 20.456 1.00 36.41 ? 104 THR B N 1 ATOM 2433 C CA . THR B 1 105 ? 5.838 6.273 20.223 1.00 30.62 ? 104 THR B CA 1 ATOM 2434 C C . THR B 1 105 ? 6.219 7.494 19.396 1.00 34.09 ? 104 THR B C 1 ATOM 2435 O O . THR B 1 105 ? 7.061 8.286 19.829 1.00 36.30 ? 104 THR B O 1 ATOM 2436 C CB . THR B 1 105 ? 5.194 6.743 21.536 1.00 24.04 ? 104 THR B CB 1 ATOM 2437 O OG1 . THR B 1 105 ? 4.504 5.670 22.174 1.00 36.06 ? 104 THR B OG1 1 ATOM 2438 C CG2 . THR B 1 105 ? 4.201 7.849 21.271 1.00 32.91 ? 104 THR B CG2 1 ATOM 2439 N N . THR B 1 106 ? 5.608 7.657 18.218 1.00 31.32 ? 105 THR B N 1 ATOM 2440 C CA . THR B 1 106 ? 5.844 8.847 17.395 1.00 34.11 ? 105 THR B CA 1 ATOM 2441 C C . THR B 1 106 ? 4.783 9.903 17.687 1.00 31.91 ? 105 THR B C 1 ATOM 2442 O O . THR B 1 106 ? 3.604 9.584 17.846 1.00 36.22 ? 105 THR B O 1 ATOM 2443 C CB . THR B 1 106 ? 5.829 8.505 15.903 1.00 34.41 ? 105 THR B CB 1 ATOM 2444 O OG1 . THR B 1 106 ? 6.707 7.401 15.664 1.00 39.42 ? 105 THR B OG1 1 ATOM 2445 C CG2 . THR B 1 106 ? 6.324 9.677 15.092 1.00 19.66 ? 105 THR B CG2 1 ATOM 2446 N N . VAL B 1 107 ? 5.203 11.163 17.777 1.00 30.71 ? 106 VAL B N 1 ATOM 2447 C CA . VAL B 1 107 ? 4.301 12.259 18.121 1.00 27.01 ? 106 VAL B CA 1 ATOM 2448 C C . VAL B 1 107 ? 4.224 13.251 16.964 1.00 28.15 ? 106 VAL B C 1 ATOM 2449 O O . VAL B 1 107 ? 5.253 13.714 16.452 1.00 25.22 ? 106 VAL B O 1 ATOM 2450 C CB . VAL B 1 107 ? 4.728 12.965 19.415 1.00 28.48 ? 106 VAL B CB 1 ATOM 2451 C CG1 . VAL B 1 107 ? 3.992 14.277 19.545 1.00 23.31 ? 106 VAL B CG1 1 ATOM 2452 C CG2 . VAL B 1 107 ? 4.443 12.080 20.604 1.00 25.75 ? 106 VAL B CG2 1 ATOM 2453 N N . THR B 1 108 ? 2.999 13.572 16.559 1.00 27.56 ? 107 THR B N 1 ATOM 2454 C CA . THR B 1 108 ? 2.716 14.587 15.556 1.00 26.43 ? 107 THR B CA 1 ATOM 2455 C C . THR B 1 108 ? 2.080 15.797 16.235 1.00 26.53 ? 107 THR B C 1 ATOM 2456 O O . THR B 1 108 ? 1.075 15.660 16.942 1.00 22.73 ? 107 THR B O 1 ATOM 2457 C CB . THR B 1 108 ? 1.792 14.007 14.481 1.00 29.65 ? 107 THR B CB 1 ATOM 2458 O OG1 . THR B 1 108 ? 2.474 12.931 13.810 1.00 25.84 ? 107 THR B OG1 1 ATOM 2459 C CG2 . THR B 1 108 ? 1.331 15.097 13.478 1.00 21.60 ? 107 THR B CG2 1 ATOM 2460 N N . VAL B 1 109 ? 2.677 16.976 16.048 1.00 21.62 ? 108 VAL B N 1 ATOM 2461 C CA . VAL B 1 109 ? 2.158 18.193 16.655 1.00 19.80 ? 108 VAL B CA 1 ATOM 2462 C C . VAL B 1 109 ? 1.178 18.837 15.685 1.00 23.83 ? 108 VAL B C 1 ATOM 2463 O O . VAL B 1 109 ? 1.490 19.042 14.510 1.00 25.41 ? 108 VAL B O 1 ATOM 2464 C CB . VAL B 1 109 ? 3.293 19.162 17.041 1.00 22.57 ? 108 VAL B CB 1 ATOM 2465 C CG1 . VAL B 1 109 ? 2.733 20.499 17.500 1.00 22.59 ? 108 VAL B CG1 1 ATOM 2466 C CG2 . VAL B 1 109 ? 4.117 18.588 18.170 1.00 18.04 ? 108 VAL B CG2 1 ATOM 2467 N N . LEU B 1 110 ? -0.016 19.141 16.175 1.00 23.88 ? 109 LEU B N 1 ATOM 2468 C CA . LEU B 1 110 ? -1.030 19.848 15.415 1.00 22.31 ? 109 LEU B CA 1 ATOM 2469 C C . LEU B 1 110 ? -1.210 21.226 16.027 1.00 20.35 ? 109 LEU B C 1 ATOM 2470 O O . LEU B 1 110 ? -0.916 21.435 17.198 1.00 19.87 ? 109 LEU B O 1 ATOM 2471 C CB . LEU B 1 110 ? -2.362 19.089 15.429 1.00 24.55 ? 109 LEU B CB 1 ATOM 2472 C CG . LEU B 1 110 ? -2.232 17.597 15.125 1.00 24.58 ? 109 LEU B CG 1 ATOM 2473 C CD1 . LEU B 1 110 ? -3.521 16.918 15.422 1.00 27.51 ? 109 LEU B CD1 1 ATOM 2474 C CD2 . LEU B 1 110 ? -1.877 17.390 13.678 1.00 25.49 ? 109 LEU B CD2 1 ATOM 2475 N N . VAL B 1 111 ? -1.684 22.162 15.217 1.00 23.27 ? 110 VAL B N 1 ATOM 2476 C CA . VAL B 1 111 ? -1.965 23.527 15.633 1.00 20.77 ? 110 VAL B CA 1 ATOM 2477 C C . VAL B 1 111 ? -3.409 23.833 15.280 1.00 20.83 ? 110 VAL B C 1 ATOM 2478 O O . VAL B 1 111 ? -3.829 23.579 14.151 1.00 26.00 ? 110 VAL B O 1 ATOM 2479 C CB . VAL B 1 111 ? -1.024 24.517 14.935 1.00 22.50 ? 110 VAL B CB 1 ATOM 2480 C CG1 . VAL B 1 111 ? -1.331 25.964 15.354 1.00 23.20 ? 110 VAL B CG1 1 ATOM 2481 C CG2 . VAL B 1 111 ? 0.388 24.137 15.206 1.00 20.30 ? 110 VAL B CG2 1 ATOM 2482 N N . GLU B 1 112 ? -4.162 24.360 16.237 1.00 24.14 ? 111 GLU B N 1 ATOM 2483 C CA . GLU B 1 112 ? -5.549 24.735 15.985 1.00 22.63 ? 111 GLU B CA 1 ATOM 2484 C C . GLU B 1 112 ? -5.587 25.940 15.050 1.00 27.90 ? 111 GLU B C 1 ATOM 2485 O O . GLU B 1 112 ? -4.808 26.883 15.234 1.00 28.13 ? 111 GLU B O 1 ATOM 2486 C CB . GLU B 1 112 ? -6.261 25.088 17.282 1.00 26.39 ? 111 GLU B CB 1 ATOM 2487 C CG . GLU B 1 112 ? -6.379 23.948 18.277 1.00 37.74 ? 111 GLU B CG 1 ATOM 2488 C CD . GLU B 1 112 ? -7.360 24.267 19.417 1.00 50.04 ? 111 GLU B CD 1 ATOM 2489 O OE1 . GLU B 1 112 ? -7.562 25.468 19.708 1.00 53.60 ? 111 GLU B OE1 1 ATOM 2490 O OE2 . GLU B 1 112 ? -7.960 23.322 19.993 1.00 45.99 ? 111 GLU B OE2 1 ATOM 2491 N N . PRO B 1 113 ? -6.447 25.942 14.036 1.00 25.40 ? 112 PRO B N 1 ATOM 2492 C CA . PRO B 1 113 ? -6.579 27.136 13.191 1.00 24.59 ? 112 PRO B CA 1 ATOM 2493 C C . PRO B 1 113 ? -7.336 28.231 13.925 1.00 24.89 ? 112 PRO B C 1 ATOM 2494 O O . PRO B 1 113 ? -8.128 27.973 14.833 1.00 24.93 ? 112 PRO B O 1 ATOM 2495 C CB . PRO B 1 113 ? -7.371 26.627 11.982 1.00 23.70 ? 112 PRO B CB 1 ATOM 2496 C CG . PRO B 1 113 ? -8.211 25.502 12.560 1.00 24.96 ? 112 PRO B CG 1 ATOM 2497 C CD . PRO B 1 113 ? -7.304 24.835 13.574 1.00 24.12 ? 112 PRO B CD 1 ATOM 2498 N N . THR B 1 114 ? -7.073 29.467 13.527 1.00 24.38 ? 113 THR B N 1 ATOM 2499 C CA . THR B 1 114 ? -7.822 30.631 13.983 1.00 21.41 ? 113 THR B CA 1 ATOM 2500 C C . THR B 1 114 ? -8.868 30.981 12.924 1.00 25.91 ? 113 THR B C 1 ATOM 2501 O O . THR B 1 114 ? -8.527 31.464 11.843 1.00 26.22 ? 113 THR B O 1 ATOM 2502 C CB . THR B 1 114 ? -6.881 31.807 14.208 1.00 27.28 ? 113 THR B CB 1 ATOM 2503 O OG1 . THR B 1 114 ? -5.794 31.414 15.060 1.00 30.81 ? 113 THR B OG1 1 ATOM 2504 C CG2 . THR B 1 114 ? -7.632 32.975 14.841 1.00 22.74 ? 113 THR B CG2 1 ATOM 2505 N N . VAL B 1 115 ? -10.126 30.763 13.231 1.00 21.73 ? 114 VAL B N 1 ATOM 2506 C CA . VAL B 1 115 ? -11.201 30.905 12.256 1.00 23.39 ? 114 VAL B CA 1 ATOM 2507 C C . VAL B 1 115 ? -11.927 32.236 12.436 1.00 33.12 ? 114 VAL B C 1 ATOM 2508 O O . VAL B 1 115 ? -12.195 32.676 13.567 1.00 36.11 ? 114 VAL B O 1 ATOM 2509 C CB . VAL B 1 115 ? -12.177 29.726 12.384 1.00 24.77 ? 114 VAL B CB 1 ATOM 2510 C CG1 . VAL B 1 115 ? -13.347 29.896 11.467 1.00 25.52 ? 114 VAL B CG1 1 ATOM 2511 C CG2 . VAL B 1 115 ? -11.449 28.446 12.088 1.00 30.34 ? 114 VAL B CG2 1 ATOM 2512 N N . SER B 1 116 ? -12.258 32.884 11.313 1.00 30.71 ? 115 SER B N 1 ATOM 2513 C CA . SER B 1 116 ? -13.121 34.061 11.303 1.00 29.12 ? 115 SER B CA 1 ATOM 2514 C C . SER B 1 116 ? -14.008 34.043 10.065 1.00 30.88 ? 115 SER B C 1 ATOM 2515 O O . SER B 1 116 ? -13.586 33.605 8.994 1.00 26.27 ? 115 SER B O 1 ATOM 2516 C CB . SER B 1 116 ? -12.319 35.377 11.348 1.00 25.69 ? 115 SER B CB 1 ATOM 2517 O OG . SER B 1 116 ? -11.459 35.513 10.241 1.00 32.66 ? 115 SER B OG 1 ATOM 2518 N N . LEU B 1 117 ? -15.244 34.515 10.215 1.00 34.13 ? 116 LEU B N 1 ATOM 2519 C CA . LEU B 1 117 ? -16.150 34.674 9.086 1.00 34.82 ? 116 LEU B CA 1 ATOM 2520 C C . LEU B 1 117 ? -16.454 36.155 8.891 1.00 36.72 ? 116 LEU B C 1 ATOM 2521 O O . LEU B 1 117 ? -16.845 36.842 9.839 1.00 35.97 ? 116 LEU B O 1 ATOM 2522 C CB . LEU B 1 117 ? -17.438 33.880 9.286 1.00 33.33 ? 116 LEU B CB 1 ATOM 2523 C CG . LEU B 1 117 ? -18.417 33.933 8.103 1.00 33.35 ? 116 LEU B CG 1 ATOM 2524 C CD1 . LEU B 1 117 ? -17.889 33.217 6.856 1.00 29.52 ? 116 LEU B CD1 1 ATOM 2525 C CD2 . LEU B 1 117 ? -19.717 33.336 8.536 1.00 31.61 ? 116 LEU B CD2 1 ATOM 2526 N N . ILE B 1 118 ? -16.280 36.644 7.665 1.00 37.55 ? 117 ILE B N 1 ATOM 2527 C CA . ILE B 1 118 ? -16.420 38.064 7.381 1.00 36.28 ? 117 ILE B CA 1 ATOM 2528 C C . ILE B 1 118 ? -17.324 38.259 6.171 1.00 39.58 ? 117 ILE B C 1 ATOM 2529 O O . ILE B 1 118 ? -17.464 37.369 5.320 1.00 36.59 ? 117 ILE B O 1 ATOM 2530 C CB . ILE B 1 118 ? -15.034 38.716 7.186 1.00 33.58 ? 117 ILE B CB 1 ATOM 2531 C CG1 . ILE B 1 118 ? -14.889 39.872 8.155 1.00 35.25 ? 117 ILE B CG1 1 ATOM 2532 C CG2 . ILE B 1 118 ? -14.784 39.142 5.747 1.00 34.49 ? 117 ILE B CG2 1 ATOM 2533 C CD1 . ILE B 1 118 ? -15.116 39.459 9.609 1.00 36.19 ? 117 ILE B CD1 1 ATOM 2534 N N . LYS B 1 119 ? -17.983 39.418 6.123 1.00 43.02 ? 118 LYS B N 1 ATOM 2535 C CA . LYS B 1 119 ? -18.839 39.741 4.987 1.00 43.85 ? 118 LYS B CA 1 ATOM 2536 C C . LYS B 1 119 ? -18.005 40.249 3.817 1.00 43.72 ? 118 LYS B C 1 ATOM 2537 O O . LYS B 1 119 ? -16.934 40.832 3.995 1.00 41.11 ? 118 LYS B O 1 ATOM 2538 C CB . LYS B 1 119 ? -19.895 40.779 5.367 1.00 46.99 ? 118 LYS B CB 1 ATOM 2539 C CG . LYS B 1 119 ? -20.972 40.255 6.299 1.00 58.06 ? 118 LYS B CG 1 ATOM 2540 C CD . LYS B 1 119 ? -21.989 41.342 6.666 1.00 57.98 ? 118 LYS B CD 1 ATOM 2541 C CE . LYS B 1 119 ? -23.067 40.804 7.612 1.00 58.61 ? 118 LYS B CE 1 ATOM 2542 N NZ . LYS B 1 119 ? -24.049 41.846 8.031 1.00 69.59 ? 118 LYS B NZ 1 ATOM 2543 N N . GLY B 1 120 ? -18.501 39.997 2.607 1.00 46.40 ? 119 GLY B N 1 ATOM 2544 C CA . GLY B 1 120 ? -17.863 40.469 1.404 1.00 44.98 ? 119 GLY B CA 1 ATOM 2545 C C . GLY B 1 120 ? -17.785 41.980 1.381 1.00 55.08 ? 119 GLY B C 1 ATOM 2546 O O . GLY B 1 120 ? -18.506 42.682 2.102 1.00 49.44 ? 119 GLY B O 1 ATOM 2547 N N . PRO B 1 121 ? -16.892 42.509 0.544 1.00 57.24 ? 120 PRO B N 1 ATOM 2548 C CA . PRO B 1 121 ? -16.671 43.963 0.532 1.00 60.76 ? 120 PRO B CA 1 ATOM 2549 C C . PRO B 1 121 ? -17.767 44.740 -0.192 1.00 70.88 ? 120 PRO B C 1 ATOM 2550 O O . PRO B 1 121 ? -18.001 45.917 0.119 1.00 64.62 ? 120 PRO B O 1 ATOM 2551 C CB . PRO B 1 121 ? -15.321 44.090 -0.180 1.00 50.33 ? 120 PRO B CB 1 ATOM 2552 C CG . PRO B 1 121 ? -15.275 42.903 -1.089 1.00 51.62 ? 120 PRO B CG 1 ATOM 2553 C CD . PRO B 1 121 ? -15.983 41.795 -0.365 1.00 49.60 ? 120 PRO B CD 1 ATOM 2554 N N . ASP B 1 122 ? -18.450 44.117 -1.147 1.00 72.22 ? 121 ASP B N 1 ATOM 2555 C CA . ASP B 1 122 ? -19.489 44.764 -1.930 1.00 69.03 ? 121 ASP B CA 1 ATOM 2556 C C . ASP B 1 122 ? -20.866 44.268 -1.502 1.00 70.10 ? 121 ASP B C 1 ATOM 2557 O O . ASP B 1 122 ? -21.030 43.115 -1.088 1.00 72.39 ? 121 ASP B O 1 ATOM 2558 C CB . ASP B 1 122 ? -19.265 44.502 -3.420 1.00 66.13 ? 121 ASP B CB 1 ATOM 2559 C CG . ASP B 1 122 ? -17.954 45.076 -3.911 1.00 72.75 ? 121 ASP B CG 1 ATOM 2560 O OD1 . ASP B 1 122 ? -17.441 46.030 -3.274 1.00 68.76 ? 121 ASP B OD1 1 ATOM 2561 O OD2 . ASP B 1 122 ? -17.439 44.571 -4.931 1.00 79.01 ? 121 ASP B OD2 1 ATOM 2562 N N . SER B 1 123 ? -21.848 45.164 -1.585 1.00 73.53 ? 122 SER B N 1 ATOM 2563 C CA . SER B 1 123 ? -23.246 44.845 -1.304 1.00 65.58 ? 122 SER B CA 1 ATOM 2564 C C . SER B 1 123 ? -23.841 43.995 -2.421 1.00 65.11 ? 122 SER B C 1 ATOM 2565 O O . SER B 1 123 ? -23.551 44.202 -3.609 1.00 64.87 ? 122 SER B O 1 ATOM 2566 C CB . SER B 1 123 ? -24.043 46.138 -1.157 1.00 64.18 ? 122 SER B CB 1 ATOM 2567 O OG . SER B 1 123 ? -23.994 46.839 -2.387 1.00 61.42 ? 122 SER B OG 1 ATOM 2568 N N . LEU B 1 124 ? -24.697 43.040 -2.049 1.00 65.92 ? 123 LEU B N 1 ATOM 2569 C CA . LEU B 1 124 ? -25.260 42.050 -2.993 1.00 63.07 ? 123 LEU B CA 1 ATOM 2570 C C . LEU B 1 124 ? -26.562 42.512 -3.641 1.00 76.33 ? 123 LEU B C 1 ATOM 2571 O O . LEU B 1 124 ? -27.659 42.204 -3.160 1.00 82.49 ? 123 LEU B O 1 ATOM 2572 C CB . LEU B 1 124 ? -25.474 40.728 -2.269 1.00 61.76 ? 123 LEU B CB 1 ATOM 2573 C CG . LEU B 1 124 ? -24.392 40.303 -1.291 1.00 71.03 ? 123 LEU B CG 1 ATOM 2574 C CD1 . LEU B 1 124 ? -24.949 39.203 -0.390 1.00 62.93 ? 123 LEU B CD1 1 ATOM 2575 C CD2 . LEU B 1 124 ? -23.183 39.899 -2.146 1.00 63.25 ? 123 LEU B CD2 1 ATOM 2576 N N . ILE B 1 125 ? -26.486 43.149 -4.798 1.00 83.00 ? 124 ILE B N 1 ATOM 2577 C CA . ILE B 1 125 ? -27.651 43.703 -5.487 1.00 74.76 ? 124 ILE B CA 1 ATOM 2578 C C . ILE B 1 125 ? -28.348 42.611 -6.283 1.00 68.59 ? 124 ILE B C 1 ATOM 2579 O O . ILE B 1 125 ? -27.675 41.929 -7.065 1.00 64.03 ? 124 ILE B O 1 ATOM 2580 C CB . ILE B 1 125 ? -27.212 44.863 -6.396 1.00 77.88 ? 124 ILE B CB 1 ATOM 2581 C CG1 . ILE B 1 125 ? -26.612 46.051 -5.641 1.00 80.56 ? 124 ILE B CG1 1 ATOM 2582 C CG2 . ILE B 1 125 ? -28.387 45.343 -7.254 1.00 81.31 ? 124 ILE B CG2 1 ATOM 2583 C CD1 . ILE B 1 125 ? -27.615 47.168 -5.218 1.00 88.97 ? 124 ILE B CD1 1 ATOM 2584 N N . ASP B 1 126 ? -29.667 42.499 -6.146 1.00 71.75 ? 125 ASP B N 1 ATOM 2585 C CA . ASP B 1 126 ? -30.446 41.515 -6.908 1.00 64.73 ? 125 ASP B CA 1 ATOM 2586 C C . ASP B 1 126 ? -30.355 41.804 -8.403 1.00 64.67 ? 125 ASP B C 1 ATOM 2587 O O . ASP B 1 126 ? -30.279 42.964 -8.830 1.00 64.72 ? 125 ASP B O 1 ATOM 2588 C CB . ASP B 1 126 ? -31.908 41.513 -6.456 1.00 58.52 ? 125 ASP B CB 1 ATOM 2589 C CG . ASP B 1 126 ? -32.759 40.436 -7.100 1.00 61.06 ? 125 ASP B CG 1 ATOM 2590 O OD1 . ASP B 1 126 ? -32.228 39.582 -7.834 1.00 66.97 ? 125 ASP B OD1 1 ATOM 2591 O OD2 . ASP B 1 126 ? -33.979 40.412 -6.859 1.00 60.48 ? 125 ASP B OD2 1 ATOM 2592 N N . GLY B 1 127 ? -30.354 40.732 -9.189 1.00 62.93 ? 126 GLY B N 1 ATOM 2593 C CA . GLY B 1 127 ? -30.063 40.790 -10.598 1.00 61.45 ? 126 GLY B CA 1 ATOM 2594 C C . GLY B 1 127 ? -28.629 41.119 -10.950 1.00 61.57 ? 126 GLY B C 1 ATOM 2595 O O . GLY B 1 127 ? -28.315 41.215 -12.141 1.00 60.71 ? 126 GLY B O 1 ATOM 2596 N N A GLY B 1 128 ? -27.744 41.289 -9.975 0.01 61.64 ? 127 GLY B N 1 ATOM 2597 N N B GLY B 1 128 ? -27.743 41.294 -9.942 0.99 61.88 ? 127 GLY B N 1 ATOM 2598 C CA A GLY B 1 128 ? -26.377 41.653 -10.268 0.01 59.92 ? 127 GLY B CA 1 ATOM 2599 C CA B GLY B 1 128 ? -26.362 41.651 -10.182 0.99 59.75 ? 127 GLY B CA 1 ATOM 2600 C C A GLY B 1 128 ? -25.517 40.469 -10.674 0.01 59.70 ? 127 GLY B C 1 ATOM 2601 C C B GLY B 1 128 ? -25.467 40.454 -10.506 0.99 60.02 ? 127 GLY B C 1 ATOM 2602 O O A GLY B 1 128 ? -25.961 39.324 -10.750 0.01 57.82 ? 127 GLY B O 1 ATOM 2603 O O B GLY B 1 128 ? -25.851 39.286 -10.384 0.99 57.95 ? 127 GLY B O 1 ATOM 2604 N N . ASN B 1 129 ? -24.246 40.766 -10.939 1.00 59.13 ? 128 ASN B N 1 ATOM 2605 C CA . ASN B 1 129 ? -23.286 39.732 -11.314 1.00 56.41 ? 128 ASN B CA 1 ATOM 2606 C C . ASN B 1 129 ? -22.769 39.008 -10.065 1.00 51.31 ? 128 ASN B C 1 ATOM 2607 O O . ASN B 1 129 ? -22.997 39.430 -8.929 1.00 50.96 ? 128 ASN B O 1 ATOM 2608 C CB . ASN B 1 129 ? -22.142 40.342 -12.139 1.00 51.91 ? 128 ASN B CB 1 ATOM 2609 C CG . ASN B 1 129 ? -22.088 41.876 -12.035 1.00 61.08 ? 128 ASN B CG 1 ATOM 2610 O OD1 . ASN B 1 129 ? -22.603 42.466 -11.082 1.00 65.41 ? 128 ASN B OD1 1 ATOM 2611 N ND2 . ASN B 1 129 ? -21.491 42.521 -13.032 1.00 56.76 ? 128 ASN B ND2 1 ATOM 2612 N N . GLU B 1 130 ? -22.095 37.879 -10.291 1.00 51.77 ? 129 GLU B N 1 ATOM 2613 C CA . GLU B 1 130 ? -21.490 37.111 -9.207 1.00 51.70 ? 129 GLU B CA 1 ATOM 2614 C C . GLU B 1 130 ? -20.713 38.010 -8.257 1.00 53.29 ? 129 GLU B C 1 ATOM 2615 O O . GLU B 1 130 ? -19.834 38.761 -8.678 1.00 51.74 ? 129 GLU B O 1 ATOM 2616 C CB . GLU B 1 130 ? -20.563 36.042 -9.777 1.00 51.34 ? 129 GLU B CB 1 ATOM 2617 C CG . GLU B 1 130 ? -20.321 34.895 -8.817 1.00 54.88 ? 129 GLU B CG 1 ATOM 2618 C CD . GLU B 1 130 ? -19.851 33.624 -9.510 1.00 62.03 ? 129 GLU B CD 1 ATOM 2619 O OE1 . GLU B 1 130 ? -19.188 33.717 -10.566 1.00 72.36 ? 129 GLU B OE1 1 ATOM 2620 O OE2 . GLU B 1 130 ? -20.154 32.524 -8.999 1.00 62.64 ? 129 GLU B OE2 1 ATOM 2621 N N . THR B 1 131 ? -21.074 37.960 -6.975 1.00 52.11 ? 130 THR B N 1 ATOM 2622 C CA . THR B 1 131 ? -20.424 38.761 -5.950 1.00 51.29 ? 130 THR B CA 1 ATOM 2623 C C . THR B 1 131 ? -19.945 37.834 -4.841 1.00 48.04 ? 130 THR B C 1 ATOM 2624 O O . THR B 1 131 ? -20.501 36.750 -4.635 1.00 46.94 ? 130 THR B O 1 ATOM 2625 C CB . THR B 1 131 ? -21.373 39.862 -5.387 1.00 38.94 ? 130 THR B CB 1 ATOM 2626 N N . VAL B 1 132 ? -18.882 38.250 -4.156 1.00 42.84 ? 131 VAL B N 1 ATOM 2627 C CA . VAL B 1 132 ? -18.389 37.537 -2.982 1.00 43.29 ? 131 VAL B CA 1 ATOM 2628 C C . VAL B 1 132 ? -19.271 37.926 -1.805 1.00 42.83 ? 131 VAL B C 1 ATOM 2629 O O . VAL B 1 132 ? -19.248 39.074 -1.355 1.00 38.40 ? 131 VAL B O 1 ATOM 2630 C CB . VAL B 1 132 ? -16.915 37.851 -2.695 1.00 44.36 ? 131 VAL B CB 1 ATOM 2631 C CG1 . VAL B 1 132 ? -16.470 37.183 -1.402 1.00 31.66 ? 131 VAL B CG1 1 ATOM 2632 C CG2 . VAL B 1 132 ? -16.046 37.394 -3.848 1.00 36.20 ? 131 VAL B CG2 1 ATOM 2633 N N . ALA B 1 133 ? -20.036 36.963 -1.289 1.00 38.39 ? 132 ALA B N 1 ATOM 2634 C CA . ALA B 1 133 ? -20.966 37.273 -0.211 1.00 45.90 ? 132 ALA B CA 1 ATOM 2635 C C . ALA B 1 133 ? -20.322 37.133 1.171 1.00 46.79 ? 132 ALA B C 1 ATOM 2636 O O . ALA B 1 133 ? -20.754 37.799 2.125 1.00 41.22 ? 132 ALA B O 1 ATOM 2637 C CB . ALA B 1 133 ? -22.207 36.388 -0.334 1.00 44.11 ? 132 ALA B CB 1 ATOM 2638 N N . ALA B 1 134 ? -19.292 36.295 1.297 1.00 44.99 ? 133 ALA B N 1 ATOM 2639 C CA . ALA B 1 134 ? -18.600 36.109 2.568 1.00 41.42 ? 133 ALA B CA 1 ATOM 2640 C C . ALA B 1 134 ? -17.223 35.502 2.323 1.00 37.93 ? 133 ALA B C 1 ATOM 2641 O O . ALA B 1 134 ? -16.955 34.907 1.274 1.00 44.91 ? 133 ALA B O 1 ATOM 2642 C CB . ALA B 1 134 ? -19.408 35.229 3.526 1.00 37.00 ? 133 ALA B CB 1 ATOM 2643 N N . VAL B 1 135 ? -16.357 35.656 3.320 1.00 35.64 ? 134 VAL B N 1 ATOM 2644 C CA . VAL B 1 135 ? -14.988 35.149 3.286 1.00 36.08 ? 134 VAL B CA 1 ATOM 2645 C C . VAL B 1 135 ? -14.707 34.427 4.598 1.00 31.70 ? 134 VAL B C 1 ATOM 2646 O O . VAL B 1 135 ? -14.781 35.033 5.675 1.00 34.43 ? 134 VAL B O 1 ATOM 2647 C CB . VAL B 1 135 ? -13.958 36.270 3.059 1.00 33.71 ? 134 VAL B CB 1 ATOM 2648 C CG1 . VAL B 1 135 ? -12.538 35.686 2.939 1.00 30.02 ? 134 VAL B CG1 1 ATOM 2649 C CG2 . VAL B 1 135 ? -14.325 37.066 1.824 1.00 36.57 ? 134 VAL B CG2 1 ATOM 2650 N N . CYS B 1 136 ? -14.368 33.142 4.505 1.00 29.93 ? 135 CYS B N 1 ATOM 2651 C CA . CYS B 1 136 ? -14.010 32.332 5.658 1.00 27.66 ? 135 CYS B CA 1 ATOM 2652 C C . CYS B 1 136 ? -12.496 32.068 5.672 1.00 35.88 ? 135 CYS B C 1 ATOM 2653 O O . CYS B 1 136 ? -11.915 31.625 4.673 1.00 28.43 ? 135 CYS B O 1 ATOM 2654 C CB . CYS B 1 136 ? -14.799 31.021 5.663 1.00 26.58 ? 135 CYS B CB 1 ATOM 2655 S SG . CYS B 1 136 ? -14.842 30.302 7.346 1.00 41.38 ? 135 CYS B SG 1 ATOM 2656 N N . VAL B 1 137 ? -11.864 32.350 6.805 1.00 26.33 ? 136 VAL B N 1 ATOM 2657 C CA . VAL B 1 137 ? -10.434 32.167 6.993 1.00 25.71 ? 136 VAL B CA 1 ATOM 2658 C C . VAL B 1 137 ? -10.222 31.170 8.122 1.00 23.82 ? 136 VAL B C 1 ATOM 2659 O O . VAL B 1 137 ? -10.879 31.256 9.164 1.00 24.87 ? 136 VAL B O 1 ATOM 2660 C CB . VAL B 1 137 ? -9.734 33.499 7.314 1.00 27.04 ? 136 VAL B CB 1 ATOM 2661 C CG1 . VAL B 1 137 ? -8.297 33.248 7.601 1.00 23.79 ? 136 VAL B CG1 1 ATOM 2662 C CG2 . VAL B 1 137 ? -9.879 34.476 6.165 1.00 21.59 ? 136 VAL B CG2 1 ATOM 2663 N N . ALA B 1 138 ? -9.333 30.211 7.905 1.00 27.20 ? 137 ALA B N 1 ATOM 2664 C CA . ALA B 1 138 ? -8.821 29.333 8.961 1.00 24.72 ? 137 ALA B CA 1 ATOM 2665 C C . ALA B 1 138 ? -7.304 29.504 8.912 1.00 24.20 ? 137 ALA B C 1 ATOM 2666 O O . ALA B 1 138 ? -6.626 28.856 8.111 1.00 24.71 ? 137 ALA B O 1 ATOM 2667 C CB . ALA B 1 138 ? -9.252 27.879 8.764 1.00 14.09 ? 137 ALA B CB 1 ATOM 2668 N N . ALA B 1 139 ? -6.792 30.401 9.751 1.00 24.38 ? 138 ALA B N 1 ATOM 2669 C CA . ALA B 1 139 ? -5.403 30.833 9.721 1.00 22.93 ? 138 ALA B CA 1 ATOM 2670 C C . ALA B 1 139 ? -4.507 29.914 10.542 1.00 26.58 ? 138 ALA B C 1 ATOM 2671 O O . ALA B 1 139 ? -4.910 29.426 11.602 1.00 22.68 ? 138 ALA B O 1 ATOM 2672 C CB . ALA B 1 139 ? -5.277 32.261 10.247 1.00 18.78 ? 138 ALA B CB 1 ATOM 2673 N N . THR B 1 140 ? -3.303 29.662 9.999 1.00 30.59 ? 139 THR B N 1 ATOM 2674 C CA . THR B 1 140 ? -2.133 29.060 10.662 1.00 24.55 ? 139 THR B CA 1 ATOM 2675 C C . THR B 1 140 ? -2.465 27.826 11.493 1.00 20.31 ? 139 THR B C 1 ATOM 2676 O O . THR B 1 140 ? -2.104 27.724 12.669 1.00 19.77 ? 139 THR B O 1 ATOM 2677 C CB . THR B 1 140 ? -1.395 30.087 11.526 1.00 33.38 ? 139 THR B CB 1 ATOM 2678 O OG1 . THR B 1 140 ? -2.293 30.692 12.464 1.00 26.82 ? 139 THR B OG1 1 ATOM 2679 C CG2 . THR B 1 140 ? -0.750 31.157 10.661 1.00 32.32 ? 139 THR B CG2 1 ATOM 2680 N N . GLY B 1 141 ? -3.130 26.867 10.857 1.00 20.46 ? 140 GLY B N 1 ATOM 2681 C CA . GLY B 1 141 ? -3.354 25.560 11.435 1.00 17.95 ? 140 GLY B CA 1 ATOM 2682 C C . GLY B 1 141 ? -2.405 24.515 10.868 1.00 23.30 ? 140 GLY B C 1 ATOM 2683 O O . GLY B 1 141 ? -1.950 24.608 9.729 1.00 21.31 ? 140 GLY B O 1 ATOM 2684 N N . LYS B 1 142 ? -2.122 23.504 11.676 1.00 19.85 ? 141 LYS B N 1 ATOM 2685 C CA . LYS B 1 142 ? -1.328 22.363 11.234 1.00 22.54 ? 141 LYS B CA 1 ATOM 2686 C C . LYS B 1 142 ? -2.088 21.059 11.483 1.00 26.21 ? 141 LYS B C 1 ATOM 2687 O O . LYS B 1 142 ? -2.469 20.756 12.621 1.00 22.88 ? 141 LYS B O 1 ATOM 2688 C CB . LYS B 1 142 ? 0.014 22.324 11.952 1.00 20.36 ? 141 LYS B CB 1 ATOM 2689 C CG . LYS B 1 142 ? 0.900 21.190 11.525 1.00 23.18 ? 141 LYS B CG 1 ATOM 2690 C CD . LYS B 1 142 ? 2.279 21.274 12.218 1.00 24.14 ? 141 LYS B CD 1 ATOM 2691 C CE . LYS B 1 142 ? 3.263 20.202 11.753 1.00 23.27 ? 141 LYS B CE 1 ATOM 2692 N NZ . LYS B 1 142 ? 2.815 18.785 11.908 1.00 29.93 ? 141 LYS B NZ 1 ATOM 2693 N N . PRO B 1 143 ? -2.371 20.312 10.412 1.00 25.48 ? 142 PRO B N 1 ATOM 2694 C CA . PRO B 1 143 ? -2.222 20.741 9.014 1.00 25.65 ? 142 PRO B CA 1 ATOM 2695 C C . PRO B 1 143 ? -3.303 21.775 8.616 1.00 21.13 ? 142 PRO B C 1 ATOM 2696 O O . PRO B 1 143 ? -4.038 22.242 9.474 1.00 19.17 ? 142 PRO B O 1 ATOM 2697 C CB . PRO B 1 143 ? -2.406 19.443 8.242 1.00 16.77 ? 142 PRO B CB 1 ATOM 2698 C CG . PRO B 1 143 ? -3.428 18.706 9.094 1.00 20.97 ? 142 PRO B CG 1 ATOM 2699 C CD . PRO B 1 143 ? -2.974 18.976 10.517 1.00 18.36 ? 142 PRO B CD 1 ATOM 2700 N N . VAL B 1 144 ? -3.408 22.120 7.333 1.00 19.97 ? 143 VAL B N 1 ATOM 2701 C CA . VAL B 1 144 ? -4.376 23.140 6.945 1.00 27.75 ? 143 VAL B CA 1 ATOM 2702 C C . VAL B 1 144 ? -5.790 22.664 7.282 1.00 30.22 ? 143 VAL B C 1 ATOM 2703 O O . VAL B 1 144 ? -6.119 21.472 7.166 1.00 22.80 ? 143 VAL B O 1 ATOM 2704 C CB . VAL B 1 144 ? -4.245 23.495 5.454 1.00 25.98 ? 143 VAL B CB 1 ATOM 2705 C CG1 . VAL B 1 144 ? -4.694 22.327 4.569 1.00 25.83 ? 143 VAL B CG1 1 ATOM 2706 C CG2 . VAL B 1 144 ? -5.038 24.745 5.144 1.00 18.98 ? 143 VAL B CG2 1 ATOM 2707 N N . ALA B 1 145 ? -6.629 23.597 7.742 1.00 26.40 ? 144 ALA B N 1 ATOM 2708 C CA . ALA B 1 145 ? -7.997 23.212 8.019 1.00 21.34 ? 144 ALA B CA 1 ATOM 2709 C C . ALA B 1 145 ? -8.710 22.884 6.713 1.00 31.61 ? 144 ALA B C 1 ATOM 2710 O O . ALA B 1 145 ? -8.197 23.101 5.605 1.00 26.16 ? 144 ALA B O 1 ATOM 2711 C CB . ALA B 1 145 ? -8.737 24.307 8.766 1.00 17.87 ? 144 ALA B CB 1 ATOM 2712 N N . GLN B 1 146 ? -9.905 22.325 6.856 1.00 30.69 ? 145 GLN B N 1 ATOM 2713 C CA . GLN B 1 146 ? -10.808 22.134 5.740 1.00 29.00 ? 145 GLN B CA 1 ATOM 2714 C C . GLN B 1 146 ? -11.979 23.092 5.921 1.00 25.74 ? 145 GLN B C 1 ATOM 2715 O O . GLN B 1 146 ? -12.466 23.260 7.037 1.00 26.85 ? 145 GLN B O 1 ATOM 2716 C CB . GLN B 1 146 ? -11.245 20.675 5.691 1.00 24.10 ? 145 GLN B CB 1 ATOM 2717 C CG . GLN B 1 146 ? -12.026 20.283 4.498 1.00 34.44 ? 145 GLN B CG 1 ATOM 2718 C CD . GLN B 1 146 ? -12.365 18.827 4.535 1.00 49.19 ? 145 GLN B CD 1 ATOM 2719 O OE1 . GLN B 1 146 ? -11.480 17.984 4.756 1.00 43.02 ? 145 GLN B OE1 1 ATOM 2720 N NE2 . GLN B 1 146 ? -13.656 18.509 4.356 1.00 45.95 ? 145 GLN B NE2 1 ATOM 2721 N N . ILE B 1 147 ? -12.390 23.766 4.845 1.00 26.38 ? 146 ILE B N 1 ATOM 2722 C CA . ILE B 1 147 ? -13.537 24.681 4.869 1.00 28.75 ? 146 ILE B CA 1 ATOM 2723 C C . ILE B 1 147 ? -14.607 24.187 3.895 1.00 37.02 ? 146 ILE B C 1 ATOM 2724 O O . ILE B 1 147 ? -14.342 24.033 2.696 1.00 35.92 ? 146 ILE B O 1 ATOM 2725 C CB . ILE B 1 147 ? -13.136 26.125 4.526 1.00 27.31 ? 146 ILE B CB 1 ATOM 2726 C CG1 . ILE B 1 147 ? -12.255 26.724 5.627 1.00 25.45 ? 146 ILE B CG1 1 ATOM 2727 C CG2 . ILE B 1 147 ? -14.377 26.994 4.272 1.00 24.39 ? 146 ILE B CG2 1 ATOM 2728 C CD1 . ILE B 1 147 ? -11.730 28.099 5.292 1.00 20.60 ? 146 ILE B CD1 1 ATOM 2729 N N . ASP B 1 148 ? -15.816 23.962 4.414 1.00 34.51 ? 147 ASP B N 1 ATOM 2730 C CA . ASP B 1 148 ? -17.007 23.677 3.628 1.00 34.24 ? 147 ASP B CA 1 ATOM 2731 C C . ASP B 1 148 ? -18.097 24.680 3.978 1.00 33.54 ? 147 ASP B C 1 ATOM 2732 O O . ASP B 1 148 ? -18.080 25.292 5.047 1.00 31.89 ? 147 ASP B O 1 ATOM 2733 C CB . ASP B 1 148 ? -17.536 22.277 3.890 1.00 32.60 ? 147 ASP B CB 1 ATOM 2734 C CG . ASP B 1 148 ? -16.526 21.234 3.587 1.00 36.21 ? 147 ASP B CG 1 ATOM 2735 O OD1 . ASP B 1 148 ? -16.390 20.907 2.390 1.00 40.42 ? 147 ASP B OD1 1 ATOM 2736 O OD2 . ASP B 1 148 ? -15.868 20.751 4.538 1.00 35.40 ? 147 ASP B OD2 1 ATOM 2737 N N . TRP B 1 149 ? -19.068 24.818 3.075 1.00 34.59 ? 148 TRP B N 1 ATOM 2738 C CA . TRP B 1 149 ? -20.149 25.787 3.209 1.00 35.04 ? 148 TRP B CA 1 ATOM 2739 C C . TRP B 1 149 ? -21.497 25.082 3.177 1.00 36.53 ? 148 TRP B C 1 ATOM 2740 O O . TRP B 1 149 ? -21.686 24.120 2.425 1.00 36.00 ? 148 TRP B O 1 ATOM 2741 C CB . TRP B 1 149 ? -20.113 26.823 2.090 1.00 34.62 ? 148 TRP B CB 1 ATOM 2742 C CG . TRP B 1 149 ? -18.902 27.723 2.079 1.00 35.46 ? 148 TRP B CG 1 ATOM 2743 C CD1 . TRP B 1 149 ? -17.716 27.517 1.416 1.00 34.72 ? 148 TRP B CD1 1 ATOM 2744 C CD2 . TRP B 1 149 ? -18.784 28.989 2.719 1.00 28.11 ? 148 TRP B CD2 1 ATOM 2745 N NE1 . TRP B 1 149 ? -16.872 28.584 1.610 1.00 35.26 ? 148 TRP B NE1 1 ATOM 2746 C CE2 . TRP B 1 149 ? -17.504 29.500 2.412 1.00 31.91 ? 148 TRP B CE2 1 ATOM 2747 C CE3 . TRP B 1 149 ? -19.639 29.749 3.512 1.00 32.26 ? 148 TRP B CE3 1 ATOM 2748 C CZ2 . TRP B 1 149 ? -17.061 30.729 2.886 1.00 31.57 ? 148 TRP B CZ2 1 ATOM 2749 C CZ3 . TRP B 1 149 ? -19.201 30.959 3.988 1.00 35.79 ? 148 TRP B CZ3 1 ATOM 2750 C CH2 . TRP B 1 149 ? -17.915 31.441 3.680 1.00 30.43 ? 148 TRP B CH2 1 ATOM 2751 N N . GLU B 1 150 ? -22.436 25.573 3.981 1.00 35.93 ? 149 GLU B N 1 ATOM 2752 C CA . GLU B 1 150 ? -23.802 25.067 3.980 1.00 45.34 ? 149 GLU B CA 1 ATOM 2753 C C . GLU B 1 150 ? -24.755 26.175 3.554 1.00 46.11 ? 149 GLU B C 1 ATOM 2754 O O . GLU B 1 150 ? -24.500 27.362 3.795 1.00 41.60 ? 149 GLU B O 1 ATOM 2755 C CB . GLU B 1 150 ? -24.201 24.501 5.353 1.00 36.74 ? 149 GLU B CB 1 ATOM 2756 C CG . GLU B 1 150 ? -23.520 23.178 5.660 1.00 41.11 ? 149 GLU B CG 1 ATOM 2757 C CD . GLU B 1 150 ? -23.728 22.730 7.087 1.00 43.03 ? 149 GLU B CD 1 ATOM 2758 O OE1 . GLU B 1 150 ? -24.467 23.433 7.803 1.00 37.82 ? 149 GLU B OE1 1 ATOM 2759 O OE2 . GLU B 1 150 ? -23.126 21.703 7.495 1.00 46.60 ? 149 GLU B OE2 1 ATOM 2760 N N . GLY B 1 151 ? -25.849 25.765 2.904 1.00 42.21 ? 150 GLY B N 1 ATOM 2761 C CA . GLY B 1 151 ? -26.753 26.677 2.222 1.00 46.26 ? 150 GLY B CA 1 ATOM 2762 C C . GLY B 1 151 ? -26.415 26.801 0.748 1.00 55.86 ? 150 GLY B C 1 ATOM 2763 O O . GLY B 1 151 ? -25.523 27.568 0.376 1.00 69.56 ? 150 GLY B O 1 ATOM 2764 N N . ASP B 1 152 ? -27.106 26.062 -0.112 1.00 50.54 ? 151 ASP B N 1 ATOM 2765 C CA . ASP B 1 152 ? -26.708 25.968 -1.518 1.00 59.84 ? 151 ASP B CA 1 ATOM 2766 C C . ASP B 1 152 ? -27.128 27.216 -2.285 1.00 54.76 ? 151 ASP B C 1 ATOM 2767 O O . ASP B 1 152 ? -28.051 27.214 -3.098 1.00 61.02 ? 151 ASP B O 1 ATOM 2768 C CB . ASP B 1 152 ? -27.302 24.728 -2.152 1.00 61.90 ? 151 ASP B CB 1 ATOM 2769 C CG . ASP B 1 152 ? -26.673 23.490 -1.640 1.00 60.04 ? 151 ASP B CG 1 ATOM 2770 O OD1 . ASP B 1 152 ? -25.541 23.600 -1.119 1.00 63.87 ? 151 ASP B OD1 1 ATOM 2771 O OD2 . ASP B 1 152 ? -27.313 22.426 -1.738 1.00 57.35 ? 151 ASP B OD2 1 ATOM 2772 N N . LEU B 1 153 ? -26.420 28.299 -2.022 1.00 48.88 ? 152 LEU B N 1 ATOM 2773 C CA . LEU B 1 153 ? -26.738 29.554 -2.665 1.00 51.11 ? 152 LEU B CA 1 ATOM 2774 C C . LEU B 1 153 ? -25.700 29.982 -3.688 1.00 56.43 ? 152 LEU B C 1 ATOM 2775 O O . LEU B 1 153 ? -25.961 30.914 -4.456 1.00 56.17 ? 152 LEU B O 1 ATOM 2776 C CB . LEU B 1 153 ? -26.932 30.644 -1.601 1.00 59.75 ? 152 LEU B CB 1 ATOM 2777 C CG . LEU B 1 153 ? -28.163 30.359 -0.723 1.00 63.33 ? 152 LEU B CG 1 ATOM 2778 C CD1 . LEU B 1 153 ? -28.109 31.063 0.629 1.00 63.22 ? 152 LEU B CD1 1 ATOM 2779 C CD2 . LEU B 1 153 ? -29.429 30.733 -1.467 1.00 60.02 ? 152 LEU B CD2 1 ATOM 2780 N N . GLY B 1 154 ? -24.552 29.311 -3.744 1.00 60.17 ? 153 GLY B N 1 ATOM 2781 C CA . GLY B 1 154 ? -23.510 29.679 -4.678 1.00 53.22 ? 153 GLY B CA 1 ATOM 2782 C C . GLY B 1 154 ? -22.376 28.681 -4.698 1.00 52.76 ? 153 GLY B C 1 ATOM 2783 O O . GLY B 1 154 ? -22.582 27.500 -4.410 1.00 57.60 ? 153 GLY B O 1 ATOM 2784 N N . GLU B 1 155 ? -21.172 29.153 -5.017 1.00 48.53 ? 154 GLU B N 1 ATOM 2785 C CA . GLU B 1 155 ? -20.006 28.304 -5.187 1.00 51.50 ? 154 GLU B CA 1 ATOM 2786 C C . GLU B 1 155 ? -18.839 28.857 -4.361 1.00 47.38 ? 154 GLU B C 1 ATOM 2787 O O . GLU B 1 155 ? -18.798 30.037 -3.997 1.00 41.73 ? 154 GLU B O 1 ATOM 2788 C CB . GLU B 1 155 ? -19.651 28.199 -6.684 1.00 53.36 ? 154 GLU B CB 1 ATOM 2789 C CG . GLU B 1 155 ? -18.647 27.116 -7.053 1.00 67.90 ? 154 GLU B CG 1 ATOM 2790 C CD . GLU B 1 155 ? -18.034 27.336 -8.436 1.00 84.84 ? 154 GLU B CD 1 ATOM 2791 O OE1 . GLU B 1 155 ? -18.773 27.761 -9.355 1.00 88.32 ? 154 GLU B OE1 1 ATOM 2792 O OE2 . GLU B 1 155 ? -16.813 27.092 -8.598 1.00 73.33 ? 154 GLU B OE2 1 ATOM 2793 N N . MET B 1 156 ? -17.881 27.987 -4.068 1.00 50.87 ? 155 MET B N 1 ATOM 2794 C CA . MET B 1 156 ? -16.737 28.314 -3.225 1.00 44.69 ? 155 MET B CA 1 ATOM 2795 C C . MET B 1 156 ? -15.453 28.414 -4.046 1.00 42.25 ? 155 MET B C 1 ATOM 2796 O O . MET B 1 156 ? -15.274 27.710 -5.042 1.00 48.03 ? 155 MET B O 1 ATOM 2797 C CB . MET B 1 156 ? -16.573 27.258 -2.130 1.00 40.55 ? 155 MET B CB 1 ATOM 2798 C CG . MET B 1 156 ? -15.205 27.169 -1.530 1.00 55.61 ? 155 MET B CG 1 ATOM 2799 S SD . MET B 1 156 ? -14.996 25.659 -0.595 1.00 74.49 ? 155 MET B SD 1 ATOM 2800 C CE . MET B 1 156 ? -13.371 25.973 0.108 1.00 52.08 ? 155 MET B CE 1 ATOM 2801 N N . GLU B 1 157 ? -14.557 29.295 -3.608 1.00 35.79 ? 156 GLU B N 1 ATOM 2802 C CA . GLU B 1 157 ? -13.226 29.452 -4.187 1.00 42.78 ? 156 GLU B CA 1 ATOM 2803 C C . GLU B 1 157 ? -12.242 29.649 -3.031 1.00 44.73 ? 156 GLU B C 1 ATOM 2804 O O . GLU B 1 157 ? -12.501 30.474 -2.144 1.00 34.53 ? 156 GLU B O 1 ATOM 2805 C CB . GLU B 1 157 ? -13.211 30.651 -5.164 1.00 35.38 ? 156 GLU B CB 1 ATOM 2806 C CG . GLU B 1 157 ? -11.916 30.892 -5.928 1.00 49.27 ? 156 GLU B CG 1 ATOM 2807 C CD . GLU B 1 157 ? -11.685 32.354 -6.314 1.00 57.65 ? 156 GLU B CD 1 ATOM 2808 O OE1 . GLU B 1 157 ? -10.559 32.708 -6.698 1.00 61.01 ? 156 GLU B OE1 1 ATOM 2809 O OE2 . GLU B 1 157 ? -12.632 33.167 -6.274 1.00 74.32 ? 156 GLU B OE2 1 ATOM 2810 N N . SER B 1 158 ? -11.116 28.906 -3.037 1.00 32.72 ? 157 SER B N 1 ATOM 2811 C CA . SER B 1 158 ? -10.163 28.938 -1.928 1.00 34.51 ? 157 SER B CA 1 ATOM 2812 C C . SER B 1 158 ? -8.703 29.036 -2.379 1.00 41.97 ? 157 SER B C 1 ATOM 2813 O O . SER B 1 158 ? -8.315 28.550 -3.449 1.00 37.35 ? 157 SER B O 1 ATOM 2814 C CB . SER B 1 158 ? -10.295 27.704 -1.056 1.00 32.80 ? 157 SER B CB 1 ATOM 2815 O OG . SER B 1 158 ? -9.802 26.564 -1.743 1.00 36.51 ? 157 SER B OG 1 ATOM 2816 N N . SER B 1 159 ? -7.886 29.633 -1.506 1.00 34.45 ? 158 SER B N 1 ATOM 2817 C CA . SER B 1 159 ? -6.433 29.591 -1.612 1.00 33.73 ? 158 SER B CA 1 ATOM 2818 C C . SER B 1 159 ? -5.810 29.179 -0.279 1.00 31.12 ? 158 SER B C 1 ATOM 2819 O O . SER B 1 159 ? -6.376 29.425 0.789 1.00 39.33 ? 158 SER B O 1 ATOM 2820 C CB . SER B 1 159 ? -5.901 30.933 -2.035 1.00 26.22 ? 158 SER B CB 1 ATOM 2821 O OG . SER B 1 159 ? -6.505 31.265 -3.255 1.00 44.49 ? 158 SER B OG 1 ATOM 2822 N N . THR B 1 160 ? -4.627 28.575 -0.347 1.00 25.75 ? 159 THR B N 1 ATOM 2823 C CA . THR B 1 160 ? -3.891 28.102 0.830 1.00 29.14 ? 159 THR B CA 1 ATOM 2824 C C . THR B 1 160 ? -2.440 28.585 0.787 1.00 28.07 ? 159 THR B C 1 ATOM 2825 O O . THR B 1 160 ? -1.770 28.453 -0.241 1.00 29.29 ? 159 THR B O 1 ATOM 2826 C CB . THR B 1 160 ? -3.924 26.568 0.905 1.00 25.32 ? 159 THR B CB 1 ATOM 2827 O OG1 . THR B 1 160 ? -5.279 26.125 0.961 1.00 26.05 ? 159 THR B OG1 1 ATOM 2828 C CG2 . THR B 1 160 ? -3.197 26.057 2.153 1.00 27.74 ? 159 THR B CG2 1 ATOM 2829 N N . THR B 1 161 ? -1.948 29.139 1.892 1.00 26.50 ? 160 THR B N 1 ATOM 2830 C CA . THR B 1 161 ? -0.530 29.479 2.015 1.00 29.66 ? 160 THR B CA 1 ATOM 2831 C C . THR B 1 161 ? 0.112 28.729 3.176 1.00 28.15 ? 160 THR B C 1 ATOM 2832 O O . THR B 1 161 ? -0.292 28.915 4.327 1.00 30.15 ? 160 THR B O 1 ATOM 2833 C CB . THR B 1 161 ? -0.321 30.962 2.227 1.00 24.65 ? 160 THR B CB 1 ATOM 2834 O OG1 . THR B 1 161 ? -0.831 31.674 1.100 1.00 32.09 ? 160 THR B OG1 1 ATOM 2835 C CG2 . THR B 1 161 ? 1.184 31.216 2.365 1.00 27.13 ? 160 THR B CG2 1 ATOM 2836 N N . SER B 1 162 ? 1.126 27.912 2.887 1.00 22.79 ? 161 SER B N 1 ATOM 2837 C CA . SER B 1 162 ? 1.843 27.186 3.932 1.00 27.09 ? 161 SER B CA 1 ATOM 2838 C C . SER B 1 162 ? 3.148 27.895 4.301 1.00 28.74 ? 161 SER B C 1 ATOM 2839 O O . SER B 1 162 ? 3.768 28.581 3.483 1.00 31.01 ? 161 SER B O 1 ATOM 2840 C CB . SER B 1 162 ? 2.101 25.733 3.524 1.00 24.71 ? 161 SER B CB 1 ATOM 2841 O OG . SER B 1 162 ? 2.649 25.604 2.220 1.00 28.46 ? 161 SER B OG 1 ATOM 2842 N N . PHE B 1 163 ? 3.532 27.759 5.565 1.00 32.67 ? 162 PHE B N 1 ATOM 2843 C CA . PHE B 1 163 ? 4.567 28.563 6.202 1.00 27.09 ? 162 PHE B CA 1 ATOM 2844 C C . PHE B 1 163 ? 5.711 27.680 6.683 1.00 22.33 ? 162 PHE B C 1 ATOM 2845 O O . PHE B 1 163 ? 5.534 26.472 6.861 1.00 26.40 ? 162 PHE B O 1 ATOM 2846 C CB . PHE B 1 163 ? 3.967 29.350 7.378 1.00 26.44 ? 162 PHE B CB 1 ATOM 2847 C CG . PHE B 1 163 ? 2.853 30.275 6.969 1.00 26.89 ? 162 PHE B CG 1 ATOM 2848 C CD1 . PHE B 1 163 ? 3.132 31.443 6.270 1.00 26.10 ? 162 PHE B CD1 1 ATOM 2849 C CD2 . PHE B 1 163 ? 1.533 29.971 7.262 1.00 23.89 ? 162 PHE B CD2 1 ATOM 2850 C CE1 . PHE B 1 163 ? 2.127 32.303 5.882 1.00 25.11 ? 162 PHE B CE1 1 ATOM 2851 C CE2 . PHE B 1 163 ? 0.511 30.814 6.868 1.00 26.62 ? 162 PHE B CE2 1 ATOM 2852 C CZ . PHE B 1 163 ? 0.805 31.988 6.171 1.00 28.44 ? 162 PHE B CZ 1 ATOM 2853 N N . PRO B 1 164 ? 6.898 28.246 6.906 1.00 31.26 ? 163 PRO B N 1 ATOM 2854 C CA . PRO B 1 164 ? 8.044 27.402 7.293 1.00 29.99 ? 163 PRO B CA 1 ATOM 2855 C C . PRO B 1 164 ? 7.785 26.534 8.500 1.00 24.58 ? 163 PRO B C 1 ATOM 2856 O O . PRO B 1 164 ? 8.263 25.392 8.526 1.00 31.84 ? 163 PRO B O 1 ATOM 2857 C CB . PRO B 1 164 ? 9.161 28.422 7.557 1.00 28.76 ? 163 PRO B CB 1 ATOM 2858 C CG . PRO B 1 164 ? 8.824 29.576 6.709 1.00 29.37 ? 163 PRO B CG 1 ATOM 2859 C CD . PRO B 1 164 ? 7.298 29.655 6.742 1.00 39.08 ? 163 PRO B CD 1 ATOM 2860 N N . ASN B 1 165 ? 7.013 27.006 9.484 1.00 24.74 ? 164 ASN B N 1 ATOM 2861 C CA . ASN B 1 165 ? 6.732 26.166 10.648 1.00 26.24 ? 164 ASN B CA 1 ATOM 2862 C C . ASN B 1 165 ? 5.683 25.083 10.358 1.00 29.74 ? 164 ASN B C 1 ATOM 2863 O O . ASN B 1 165 ? 5.302 24.343 11.270 1.00 30.31 ? 164 ASN B O 1 ATOM 2864 C CB . ASN B 1 165 ? 6.330 27.033 11.858 1.00 18.58 ? 164 ASN B CB 1 ATOM 2865 C CG . ASN B 1 165 ? 5.018 27.813 11.646 1.00 33.48 ? 164 ASN B CG 1 ATOM 2866 O OD1 . ASN B 1 165 ? 4.168 27.428 10.839 1.00 29.05 ? 164 ASN B OD1 1 ATOM 2867 N ND2 . ASN B 1 165 ? 4.843 28.908 12.406 1.00 31.09 ? 164 ASN B ND2 1 ATOM 2868 N N . GLU B 1 166 ? 5.218 24.971 9.118 1.00 25.73 ? 165 GLU B N 1 ATOM 2869 C CA . GLU B 1 166 ? 4.347 23.914 8.624 1.00 30.35 ? 165 GLU B CA 1 ATOM 2870 C C . GLU B 1 166 ? 2.885 24.113 8.994 1.00 27.58 ? 165 GLU B C 1 ATOM 2871 O O . GLU B 1 166 ? 2.097 23.174 8.847 1.00 30.22 ? 165 GLU B O 1 ATOM 2872 C CB . GLU B 1 166 ? 4.781 22.530 9.102 1.00 29.77 ? 165 GLU B CB 1 ATOM 2873 C CG . GLU B 1 166 ? 6.170 22.134 8.680 1.00 28.62 ? 165 GLU B CG 1 ATOM 2874 C CD . GLU B 1 166 ? 6.348 20.646 8.780 1.00 37.36 ? 165 GLU B CD 1 ATOM 2875 O OE1 . GLU B 1 166 ? 5.692 19.910 8.009 1.00 45.78 ? 165 GLU B OE1 1 ATOM 2876 O OE2 . GLU B 1 166 ? 7.103 20.200 9.658 1.00 48.18 ? 165 GLU B OE2 1 ATOM 2877 N N . THR B 1 167 ? 2.513 25.267 9.517 1.00 19.47 ? 166 THR B N 1 ATOM 2878 C CA . THR B 1 167 ? 1.124 25.649 9.563 1.00 22.93 ? 166 THR B CA 1 ATOM 2879 C C . THR B 1 167 ? 0.723 26.251 8.215 1.00 29.68 ? 166 THR B C 1 ATOM 2880 O O . THR B 1 167 ? 1.562 26.630 7.389 1.00 27.92 ? 166 THR B O 1 ATOM 2881 C CB . THR B 1 167 ? 0.841 26.639 10.699 1.00 22.05 ? 166 THR B CB 1 ATOM 2882 O OG1 . THR B 1 167 ? 1.463 27.895 10.428 1.00 23.16 ? 166 THR B OG1 1 ATOM 2883 C CG2 . THR B 1 167 ? 1.345 26.101 12.012 1.00 27.04 ? 166 THR B CG2 1 ATOM 2884 N N . ALA B 1 168 ? -0.585 26.317 7.997 1.00 26.91 ? 167 ALA B N 1 ATOM 2885 C CA . ALA B 1 168 ? -1.137 26.783 6.738 1.00 27.05 ? 167 ALA B CA 1 ATOM 2886 C C . ALA B 1 168 ? -2.400 27.583 7.028 1.00 27.71 ? 167 ALA B C 1 ATOM 2887 O O . ALA B 1 168 ? -3.173 27.236 7.926 1.00 31.12 ? 167 ALA B O 1 ATOM 2888 C CB . ALA B 1 168 ? -1.412 25.589 5.800 1.00 19.19 ? 167 ALA B CB 1 ATOM 2889 N N . THR B 1 169 ? -2.587 28.670 6.288 1.00 27.94 ? 168 THR B N 1 ATOM 2890 C CA . THR B 1 169 ? -3.805 29.478 6.325 1.00 26.00 ? 168 THR B CA 1 ATOM 2891 C C . THR B 1 169 ? -4.604 29.247 5.051 1.00 26.64 ? 168 THR B C 1 ATOM 2892 O O . THR B 1 169 ? -4.047 29.331 3.951 1.00 29.59 ? 168 THR B O 1 ATOM 2893 C CB . THR B 1 169 ? -3.471 30.964 6.434 1.00 28.49 ? 168 THR B CB 1 ATOM 2894 O OG1 . THR B 1 169 ? -2.870 31.229 7.707 1.00 26.61 ? 168 THR B OG1 1 ATOM 2895 C CG2 . THR B 1 169 ? -4.744 31.809 6.251 1.00 27.47 ? 168 THR B CG2 1 ATOM 2896 N N . ILE B 1 170 ? -5.895 28.957 5.179 1.00 23.23 ? 169 ILE B N 1 ATOM 2897 C CA . ILE B 1 170 ? -6.736 28.792 3.999 1.00 23.74 ? 169 ILE B CA 1 ATOM 2898 C C . ILE B 1 170 ? -7.793 29.882 4.003 1.00 26.82 ? 169 ILE B C 1 ATOM 2899 O O . ILE B 1 170 ? -8.438 30.142 5.032 1.00 22.78 ? 169 ILE B O 1 ATOM 2900 C CB . ILE B 1 170 ? -7.372 27.393 3.873 1.00 17.85 ? 169 ILE B CB 1 ATOM 2901 C CG1 . ILE B 1 170 ? -8.307 27.417 2.643 1.00 26.21 ? 169 ILE B CG1 1 ATOM 2902 C CG2 . ILE B 1 170 ? -8.105 26.970 5.140 1.00 12.61 ? 169 ILE B CG2 1 ATOM 2903 C CD1 . ILE B 1 170 ? -9.005 26.112 2.298 1.00 22.28 ? 169 ILE B CD1 1 ATOM 2904 N N . VAL B 1 171 ? -7.933 30.545 2.861 1.00 25.64 ? 170 VAL B N 1 ATOM 2905 C CA . VAL B 1 171 ? -8.909 31.609 2.669 1.00 28.40 ? 170 VAL B CA 1 ATOM 2906 C C . VAL B 1 171 ? -9.917 31.127 1.623 1.00 32.41 ? 170 VAL B C 1 ATOM 2907 O O . VAL B 1 171 ? -9.536 30.785 0.489 1.00 33.51 ? 170 VAL B O 1 ATOM 2908 C CB . VAL B 1 171 ? -8.216 32.918 2.259 1.00 26.39 ? 170 VAL B CB 1 ATOM 2909 C CG1 . VAL B 1 171 ? -9.222 34.008 1.963 1.00 23.66 ? 170 VAL B CG1 1 ATOM 2910 C CG2 . VAL B 1 171 ? -7.293 33.357 3.358 1.00 24.61 ? 170 VAL B CG2 1 ATOM 2911 N N . SER B 1 172 ? -11.195 31.066 2.012 1.00 25.38 ? 171 SER B N 1 ATOM 2912 C CA . SER B 1 172 ? -12.273 30.595 1.140 1.00 29.75 ? 171 SER B CA 1 ATOM 2913 C C . SER B 1 172 ? -13.339 31.675 0.991 1.00 33.41 ? 171 SER B C 1 ATOM 2914 O O . SER B 1 172 ? -13.911 32.121 1.992 1.00 34.45 ? 171 SER B O 1 ATOM 2915 C CB . SER B 1 172 ? -12.886 29.310 1.684 1.00 31.15 ? 171 SER B CB 1 ATOM 2916 O OG . SER B 1 172 ? -14.046 28.960 0.955 1.00 40.90 ? 171 SER B OG 1 ATOM 2917 N N . GLN B 1 173 ? -13.589 32.100 -0.256 1.00 35.32 ? 172 GLN B N 1 ATOM 2918 C CA . GLN B 1 173 ? -14.636 33.068 -0.606 1.00 38.52 ? 172 GLN B CA 1 ATOM 2919 C C . GLN B 1 173 ? -15.869 32.358 -1.160 1.00 41.56 ? 172 GLN B C 1 ATOM 2920 O O . GLN B 1 173 ? -15.755 31.442 -1.981 1.00 40.70 ? 172 GLN B O 1 ATOM 2921 C CB . GLN B 1 173 ? -14.149 34.073 -1.655 1.00 36.76 ? 172 GLN B CB 1 ATOM 2922 C CG . GLN B 1 173 ? -13.088 35.057 -1.199 1.00 39.50 ? 172 GLN B CG 1 ATOM 2923 C CD . GLN B 1 173 ? -12.357 35.703 -2.366 1.00 49.53 ? 172 GLN B CD 1 ATOM 2924 O OE1 . GLN B 1 173 ? -12.697 35.474 -3.531 1.00 49.57 ? 172 GLN B OE1 1 ATOM 2925 N NE2 . GLN B 1 173 ? -11.320 36.484 -2.061 1.00 62.71 ? 172 GLN B NE2 1 ATOM 2926 N N . TYR B 1 174 ? -17.047 32.791 -0.720 1.00 33.99 ? 173 TYR B N 1 ATOM 2927 C CA . TYR B 1 174 ? -18.303 32.234 -1.204 1.00 38.89 ? 173 TYR B CA 1 ATOM 2928 C C . TYR B 1 174 ? -18.924 33.209 -2.202 1.00 47.65 ? 173 TYR B C 1 ATOM 2929 O O . TYR B 1 174 ? -19.232 34.359 -1.849 1.00 40.09 ? 173 TYR B O 1 ATOM 2930 C CB . TYR B 1 174 ? -19.259 31.949 -0.048 1.00 36.73 ? 173 TYR B CB 1 ATOM 2931 C CG . TYR B 1 174 ? -20.329 30.940 -0.404 1.00 45.38 ? 173 TYR B CG 1 ATOM 2932 C CD1 . TYR B 1 174 ? -20.010 29.601 -0.591 1.00 40.34 ? 173 TYR B CD1 1 ATOM 2933 C CD2 . TYR B 1 174 ? -21.656 31.325 -0.557 1.00 48.48 ? 173 TYR B CD2 1 ATOM 2934 C CE1 . TYR B 1 174 ? -20.979 28.684 -0.919 1.00 48.28 ? 173 TYR B CE1 1 ATOM 2935 C CE2 . TYR B 1 174 ? -22.627 30.413 -0.886 1.00 41.51 ? 173 TYR B CE2 1 ATOM 2936 C CZ . TYR B 1 174 ? -22.287 29.101 -1.066 1.00 46.85 ? 173 TYR B CZ 1 ATOM 2937 O OH . TYR B 1 174 ? -23.253 28.187 -1.391 1.00 51.18 ? 173 TYR B OH 1 ATOM 2938 N N . LYS B 1 175 ? -19.085 32.755 -3.447 1.00 48.04 ? 174 LYS B N 1 ATOM 2939 C CA . LYS B 1 175 ? -19.586 33.583 -4.540 1.00 51.81 ? 174 LYS B CA 1 ATOM 2940 C C . LYS B 1 175 ? -21.006 33.175 -4.891 1.00 53.53 ? 174 LYS B C 1 ATOM 2941 O O . LYS B 1 175 ? -21.316 31.978 -4.947 1.00 50.82 ? 174 LYS B O 1 ATOM 2942 C CB . LYS B 1 175 ? -18.712 33.448 -5.786 1.00 50.57 ? 174 LYS B CB 1 ATOM 2943 C CG . LYS B 1 175 ? -17.395 34.189 -5.700 1.00 57.07 ? 174 LYS B CG 1 ATOM 2944 C CD . LYS B 1 175 ? -16.258 33.347 -6.271 1.00 57.22 ? 174 LYS B CD 1 ATOM 2945 C CE . LYS B 1 175 ? -16.451 33.125 -7.762 1.00 67.88 ? 174 LYS B CE 1 ATOM 2946 N NZ . LYS B 1 175 ? -15.718 34.132 -8.580 1.00 71.16 ? 174 LYS B NZ 1 ATOM 2947 N N . LEU B 1 176 ? -21.862 34.169 -5.142 1.00 55.17 ? 175 LEU B N 1 ATOM 2948 C CA . LEU B 1 176 ? -23.228 33.899 -5.592 1.00 58.20 ? 175 LEU B CA 1 ATOM 2949 C C . LEU B 1 176 ? -23.765 35.054 -6.433 1.00 46.72 ? 175 LEU B C 1 ATOM 2950 O O . LEU B 1 176 ? -23.349 36.209 -6.283 1.00 39.15 ? 175 LEU B O 1 ATOM 2951 C CB . LEU B 1 176 ? -24.175 33.630 -4.410 1.00 48.61 ? 175 LEU B CB 1 ATOM 2952 C CG . LEU B 1 176 ? -24.275 34.649 -3.261 1.00 52.98 ? 175 LEU B CG 1 ATOM 2953 C CD1 . LEU B 1 176 ? -25.070 35.878 -3.631 1.00 52.01 ? 175 LEU B CD1 1 ATOM 2954 C CD2 . LEU B 1 176 ? -24.892 34.010 -2.031 1.00 53.69 ? 175 LEU B CD2 1 ATOM 2955 N N . PHE B 1 177 ? -24.708 34.720 -7.320 1.00 50.56 ? 176 PHE B N 1 ATOM 2956 C CA . PHE B 1 177 ? -25.520 35.726 -7.995 1.00 52.31 ? 176 PHE B CA 1 ATOM 2957 C C . PHE B 1 177 ? -26.688 36.052 -7.078 1.00 49.73 ? 176 PHE B C 1 ATOM 2958 O O . PHE B 1 177 ? -27.523 35.166 -6.819 1.00 49.28 ? 176 PHE B O 1 ATOM 2959 C CB . PHE B 1 177 ? -26.028 35.222 -9.342 1.00 55.45 ? 176 PHE B CB 1 ATOM 2960 C CG . PHE B 1 177 ? -24.945 34.742 -10.269 1.00 53.13 ? 176 PHE B CG 1 ATOM 2961 C CD1 . PHE B 1 177 ? -24.521 33.415 -10.228 1.00 52.58 ? 176 PHE B CD1 1 ATOM 2962 C CD2 . PHE B 1 177 ? -24.372 35.605 -11.196 1.00 49.04 ? 176 PHE B CD2 1 ATOM 2963 C CE1 . PHE B 1 177 ? -23.531 32.962 -11.069 1.00 57.14 ? 176 PHE B CE1 1 ATOM 2964 C CE2 . PHE B 1 177 ? -23.376 35.162 -12.042 1.00 57.40 ? 176 PHE B CE2 1 ATOM 2965 C CZ . PHE B 1 177 ? -22.951 33.836 -11.982 1.00 65.66 ? 176 PHE B CZ 1 ATOM 2966 N N . PRO B 1 178 ? -26.777 37.269 -6.541 1.00 40.45 ? 177 PRO B N 1 ATOM 2967 C CA . PRO B 1 178 ? -27.882 37.587 -5.632 1.00 47.44 ? 177 PRO B CA 1 ATOM 2968 C C . PRO B 1 178 ? -29.226 37.481 -6.347 1.00 55.60 ? 177 PRO B C 1 ATOM 2969 O O . PRO B 1 178 ? -29.383 37.951 -7.476 1.00 58.99 ? 177 PRO B O 1 ATOM 2970 C CB . PRO B 1 178 ? -27.583 39.031 -5.206 1.00 50.93 ? 177 PRO B CB 1 ATOM 2971 C CG . PRO B 1 178 ? -26.145 39.263 -5.549 1.00 46.41 ? 177 PRO B CG 1 ATOM 2972 C CD . PRO B 1 178 ? -25.894 38.423 -6.763 1.00 38.07 ? 177 PRO B CD 1 ATOM 2973 N N . THR B 1 179 ? -30.198 36.843 -5.688 1.00 59.31 ? 178 THR B N 1 ATOM 2974 C CA . THR B 1 179 ? -31.564 36.763 -6.201 1.00 59.99 ? 178 THR B CA 1 ATOM 2975 C C . THR B 1 179 ? -32.571 36.939 -5.071 1.00 66.39 ? 178 THR B C 1 ATOM 2976 O O . THR B 1 179 ? -32.225 37.025 -3.890 1.00 68.64 ? 178 THR B O 1 ATOM 2977 C CB . THR B 1 179 ? -31.873 35.432 -6.905 1.00 51.07 ? 178 THR B CB 1 ATOM 2978 O OG1 . THR B 1 179 ? -31.764 34.350 -5.973 1.00 60.70 ? 178 THR B OG1 1 ATOM 2979 C CG2 . THR B 1 179 ? -30.947 35.197 -8.070 1.00 60.75 ? 178 THR B CG2 1 ATOM 2980 N N . ARG B 1 180 ? -33.843 36.992 -5.465 1.00 66.01 ? 179 ARG B N 1 ATOM 2981 C CA . ARG B 1 180 ? -34.917 37.010 -4.487 1.00 66.02 ? 179 ARG B CA 1 ATOM 2982 C C . ARG B 1 180 ? -34.922 35.730 -3.664 1.00 66.19 ? 179 ARG B C 1 ATOM 2983 O O . ARG B 1 180 ? -35.149 35.767 -2.448 1.00 63.51 ? 179 ARG B O 1 ATOM 2984 C CB . ARG B 1 180 ? -36.256 37.205 -5.200 1.00 75.10 ? 179 ARG B CB 1 ATOM 2985 C CG . ARG B 1 180 ? -37.383 37.771 -4.328 1.00 83.44 ? 179 ARG B CG 1 ATOM 2986 C CD . ARG B 1 180 ? -36.868 38.724 -3.227 1.00 86.68 ? 179 ARG B CD 1 ATOM 2987 N NE . ARG B 1 180 ? -36.069 39.836 -3.758 1.00 85.96 ? 179 ARG B NE 1 ATOM 2988 C CZ . ARG B 1 180 ? -35.732 40.927 -3.075 1.00 85.56 ? 179 ARG B CZ 1 ATOM 2989 N NH1 . ARG B 1 180 ? -36.155 41.092 -1.840 1.00 79.98 ? 179 ARG B NH1 1 ATOM 2990 N NH2 . ARG B 1 180 ? -35.002 41.879 -3.641 1.00 79.31 ? 179 ARG B NH2 1 ATOM 2991 N N . PHE B 1 181 ? -34.669 34.587 -4.317 1.00 54.05 ? 180 PHE B N 1 ATOM 2992 C CA . PHE B 1 181 ? -34.756 33.296 -3.640 1.00 64.56 ? 180 PHE B CA 1 ATOM 2993 C C . PHE B 1 181 ? -33.730 33.169 -2.520 1.00 74.18 ? 180 PHE B C 1 ATOM 2994 O O . PHE B 1 181 ? -33.980 32.474 -1.524 1.00 73.50 ? 180 PHE B O 1 ATOM 2995 C CB . PHE B 1 181 ? -34.588 32.158 -4.654 1.00 69.35 ? 180 PHE B CB 1 ATOM 2996 C CG . PHE B 1 181 ? -34.453 30.798 -4.022 1.00 74.75 ? 180 PHE B CG 1 ATOM 2997 C CD1 . PHE B 1 181 ? -35.552 30.150 -3.490 1.00 72.29 ? 180 PHE B CD1 1 ATOM 2998 C CD2 . PHE B 1 181 ? -33.219 30.175 -3.948 1.00 80.43 ? 180 PHE B CD2 1 ATOM 2999 C CE1 . PHE B 1 181 ? -35.420 28.903 -2.901 1.00 78.74 ? 180 PHE B CE1 1 ATOM 3000 C CE2 . PHE B 1 181 ? -33.085 28.933 -3.363 1.00 75.38 ? 180 PHE B CE2 1 ATOM 3001 C CZ . PHE B 1 181 ? -34.185 28.298 -2.838 1.00 75.87 ? 180 PHE B CZ 1 ATOM 3002 N N . ALA B 1 182 ? -32.583 33.838 -2.659 1.00 70.78 ? 181 ALA B N 1 ATOM 3003 C CA . ALA B 1 182 ? -31.512 33.790 -1.677 1.00 64.02 ? 181 ALA B CA 1 ATOM 3004 C C . ALA B 1 182 ? -31.699 34.781 -0.544 1.00 61.35 ? 181 ALA B C 1 ATOM 3005 O O . ALA B 1 182 ? -30.989 34.686 0.462 1.00 68.98 ? 181 ALA B O 1 ATOM 3006 C CB . ALA B 1 182 ? -30.158 34.053 -2.351 1.00 63.98 ? 181 ALA B CB 1 ATOM 3007 N N . ARG B 1 183 ? -32.619 35.726 -0.671 1.00 67.57 ? 182 ARG B N 1 ATOM 3008 C CA . ARG B 1 183 ? -32.778 36.726 0.375 1.00 71.63 ? 182 ARG B CA 1 ATOM 3009 C C . ARG B 1 183 ? -33.268 36.084 1.662 1.00 65.16 ? 182 ARG B C 1 ATOM 3010 O O . ARG B 1 183 ? -34.048 35.130 1.643 1.00 57.12 ? 182 ARG B O 1 ATOM 3011 C CB . ARG B 1 183 ? -33.750 37.813 -0.059 1.00 64.15 ? 182 ARG B CB 1 ATOM 3012 C CG . ARG B 1 183 ? -33.870 38.942 0.947 1.00 76.30 ? 182 ARG B CG 1 ATOM 3013 C CD . ARG B 1 183 ? -34.911 39.881 0.464 1.00 77.19 ? 182 ARG B CD 1 ATOM 3014 N NE . ARG B 1 183 ? -35.468 40.768 1.470 1.00 79.13 ? 182 ARG B NE 1 ATOM 3015 C CZ . ARG B 1 183 ? -36.736 41.157 1.452 1.00 83.78 ? 182 ARG B CZ 1 ATOM 3016 N NH1 . ARG B 1 183 ? -37.542 40.686 0.509 1.00 85.57 ? 182 ARG B NH1 1 ATOM 3017 N NH2 . ARG B 1 183 ? -37.206 41.980 2.381 1.00 82.73 ? 182 ARG B NH2 1 ATOM 3018 N N . GLY B 1 184 ? -32.787 36.605 2.788 1.00 68.79 ? 183 GLY B N 1 ATOM 3019 C CA . GLY B 1 184 ? -33.189 36.119 4.084 1.00 71.56 ? 183 GLY B CA 1 ATOM 3020 C C . GLY B 1 184 ? -32.611 34.782 4.491 1.00 68.06 ? 183 GLY B C 1 ATOM 3021 O O . GLY B 1 184 ? -32.761 34.396 5.655 1.00 68.18 ? 183 GLY B O 1 ATOM 3022 N N . ARG B 1 185 ? -31.955 34.063 3.585 1.00 63.85 ? 184 ARG B N 1 ATOM 3023 C CA . ARG B 1 185 ? -31.410 32.763 3.939 1.00 69.66 ? 184 ARG B CA 1 ATOM 3024 C C . ARG B 1 185 ? -30.006 32.899 4.550 1.00 57.68 ? 184 ARG B C 1 ATOM 3025 O O . ARG B 1 185 ? -29.323 33.922 4.411 1.00 51.54 ? 184 ARG B O 1 ATOM 3026 C CB . ARG B 1 185 ? -31.409 31.839 2.714 1.00 66.44 ? 184 ARG B CB 1 ATOM 3027 C CG . ARG B 1 185 ? -32.815 31.474 2.219 1.00 60.51 ? 184 ARG B CG 1 ATOM 3028 C CD . ARG B 1 185 ? -32.753 30.628 0.970 1.00 64.79 ? 184 ARG B CD 1 ATOM 3029 N NE . ARG B 1 185 ? -32.055 29.373 1.223 1.00 83.19 ? 184 ARG B NE 1 ATOM 3030 C CZ . ARG B 1 185 ? -32.657 28.212 1.464 1.00 85.61 ? 184 ARG B CZ 1 ATOM 3031 N NH1 . ARG B 1 185 ? -33.983 28.137 1.469 1.00 84.33 ? 184 ARG B NH1 1 ATOM 3032 N NH2 . ARG B 1 185 ? -31.931 27.121 1.685 1.00 83.87 ? 184 ARG B NH2 1 ATOM 3033 N N . ARG B 1 186 ? -29.595 31.844 5.255 1.00 57.43 ? 185 ARG B N 1 ATOM 3034 C CA . ARG B 1 186 ? -28.376 31.822 6.058 1.00 53.90 ? 185 ARG B CA 1 ATOM 3035 C C . ARG B 1 186 ? -27.297 31.005 5.360 1.00 45.76 ? 185 ARG B C 1 ATOM 3036 O O . ARG B 1 186 ? -27.560 29.883 4.916 1.00 38.00 ? 185 ARG B O 1 ATOM 3037 C CB . ARG B 1 186 ? -28.654 31.229 7.441 1.00 49.99 ? 185 ARG B CB 1 ATOM 3038 C CG . ARG B 1 186 ? -27.412 30.962 8.275 1.00 49.80 ? 185 ARG B CG 1 ATOM 3039 C CD . ARG B 1 186 ? -27.735 30.321 9.634 1.00 46.45 ? 185 ARG B CD 1 ATOM 3040 N NE . ARG B 1 186 ? -28.788 31.029 10.358 1.00 52.00 ? 185 ARG B NE 1 ATOM 3041 C CZ . ARG B 1 186 ? -28.620 32.134 11.080 1.00 55.34 ? 185 ARG B CZ 1 ATOM 3042 N NH1 . ARG B 1 186 ? -27.427 32.705 11.191 1.00 43.00 ? 185 ARG B NH1 1 ATOM 3043 N NH2 . ARG B 1 186 ? -29.666 32.679 11.690 1.00 66.14 ? 185 ARG B NH2 1 ATOM 3044 N N . ILE B 1 187 ? -26.090 31.575 5.257 1.00 44.76 ? 186 ILE B N 1 ATOM 3045 C CA . ILE B 1 187 ? -24.912 30.850 4.780 1.00 40.00 ? 186 ILE B CA 1 ATOM 3046 C C . ILE B 1 187 ? -23.999 30.559 5.961 1.00 42.82 ? 186 ILE B C 1 ATOM 3047 O O . ILE B 1 187 ? -23.687 31.456 6.767 1.00 32.86 ? 186 ILE B O 1 ATOM 3048 C CB . ILE B 1 187 ? -24.140 31.621 3.690 1.00 39.61 ? 186 ILE B CB 1 ATOM 3049 C CG1 . ILE B 1 187 ? -23.747 33.021 4.166 1.00 42.52 ? 186 ILE B CG1 1 ATOM 3050 C CG2 . ILE B 1 187 ? -24.901 31.632 2.368 1.00 50.26 ? 186 ILE B CG2 1 ATOM 3051 C CD1 . ILE B 1 187 ? -22.775 33.703 3.237 1.00 39.55 ? 186 ILE B CD1 1 ATOM 3052 N N . THR B 1 188 ? -23.536 29.309 6.031 1.00 41.38 ? 187 THR B N 1 ATOM 3053 C CA . THR B 1 188 ? -22.717 28.797 7.121 1.00 38.90 ? 187 THR B CA 1 ATOM 3054 C C . THR B 1 188 ? -21.345 28.374 6.605 1.00 37.32 ? 187 THR B C 1 ATOM 3055 O O . THR B 1 188 ? -21.251 27.663 5.599 1.00 31.53 ? 187 THR B O 1 ATOM 3056 C CB . THR B 1 188 ? -23.404 27.605 7.794 1.00 39.48 ? 187 THR B CB 1 ATOM 3057 O OG1 . THR B 1 188 ? -24.658 28.030 8.357 1.00 45.24 ? 187 THR B OG1 1 ATOM 3058 C CG2 . THR B 1 188 ? -22.508 27.015 8.893 1.00 36.44 ? 187 THR B CG2 1 ATOM 3059 N N . CYS B 1 189 ? -20.295 28.822 7.301 1.00 34.09 ? 188 CYS B N 1 ATOM 3060 C CA . CYS B 1 189 ? -18.920 28.371 7.120 1.00 33.00 ? 188 CYS B CA 1 ATOM 3061 C C . CYS B 1 189 ? -18.597 27.272 8.141 1.00 38.54 ? 188 CYS B C 1 ATOM 3062 O O . CYS B 1 189 ? -18.749 27.471 9.351 1.00 34.49 ? 188 CYS B O 1 ATOM 3063 C CB . CYS B 1 189 ? -17.929 29.533 7.297 1.00 36.57 ? 188 CYS B CB 1 ATOM 3064 S SG . CYS B 1 189 ? -16.292 28.873 7.381 1.00 51.08 ? 188 CYS B SG 1 ATOM 3065 N N . VAL B 1 190 ? -18.103 26.137 7.663 1.00 31.39 ? 189 VAL B N 1 ATOM 3066 C CA . VAL B 1 190 ? -17.867 24.965 8.500 1.00 33.64 ? 189 VAL B CA 1 ATOM 3067 C C . VAL B 1 190 ? -16.385 24.590 8.390 1.00 35.67 ? 189 VAL B C 1 ATOM 3068 O O . VAL B 1 190 ? -15.899 24.252 7.300 1.00 32.79 ? 189 VAL B O 1 ATOM 3069 C CB . VAL B 1 190 ? -18.794 23.805 8.092 1.00 32.95 ? 189 VAL B CB 1 ATOM 3070 C CG1 . VAL B 1 190 ? -18.495 22.521 8.880 1.00 28.29 ? 189 VAL B CG1 1 ATOM 3071 C CG2 . VAL B 1 190 ? -20.241 24.233 8.290 1.00 33.41 ? 189 VAL B CG2 1 ATOM 3072 N N . VAL B 1 191 ? -15.668 24.663 9.511 1.00 29.69 ? 190 VAL B N 1 ATOM 3073 C CA . VAL B 1 191 ? -14.225 24.443 9.545 1.00 25.65 ? 190 VAL B CA 1 ATOM 3074 C C . VAL B 1 191 ? -13.963 23.156 10.315 1.00 26.54 ? 190 VAL B C 1 ATOM 3075 O O . VAL B 1 191 ? -14.302 23.053 11.502 1.00 21.46 ? 190 VAL B O 1 ATOM 3076 C CB . VAL B 1 191 ? -13.478 25.629 10.179 1.00 29.62 ? 190 VAL B CB 1 ATOM 3077 C CG1 . VAL B 1 191 ? -11.974 25.353 10.229 1.00 23.70 ? 190 VAL B CG1 1 ATOM 3078 C CG2 . VAL B 1 191 ? -13.750 26.911 9.422 1.00 21.81 ? 190 VAL B CG2 1 ATOM 3079 N N . LYS B 1 192 ? -13.367 22.178 9.634 1.00 27.60 ? 191 LYS B N 1 ATOM 3080 C CA . LYS B 1 192 ? -13.021 20.880 10.205 1.00 30.84 ? 191 LYS B CA 1 ATOM 3081 C C . LYS B 1 192 ? -11.508 20.806 10.377 1.00 26.38 ? 191 LYS B C 1 ATOM 3082 O O . LYS B 1 192 ? -10.765 21.199 9.472 1.00 24.50 ? 191 LYS B O 1 ATOM 3083 C CB . LYS B 1 192 ? -13.519 19.736 9.310 1.00 20.44 ? 191 LYS B CB 1 ATOM 3084 C CG . LYS B 1 192 ? -13.037 18.368 9.759 1.00 31.30 ? 191 LYS B CG 1 ATOM 3085 C CD . LYS B 1 192 ? -13.701 17.222 8.995 1.00 35.91 ? 191 LYS B CD 1 ATOM 3086 C CE . LYS B 1 192 ? -13.620 17.448 7.493 1.00 42.40 ? 191 LYS B CE 1 ATOM 3087 N NZ . LYS B 1 192 ? -14.335 16.405 6.703 1.00 51.43 ? 191 LYS B NZ 1 ATOM 3088 N N . HIS B 1 193 ? -11.051 20.316 11.541 1.00 27.27 ? 192 HIS B N 1 ATOM 3089 C CA . HIS B 1 193 ? -9.611 20.191 11.775 1.00 20.00 ? 192 HIS B CA 1 ATOM 3090 C C . HIS B 1 193 ? -9.342 19.152 12.850 1.00 22.62 ? 192 HIS B C 1 ATOM 3091 O O . HIS B 1 193 ? -10.059 19.131 13.857 1.00 20.67 ? 192 HIS B O 1 ATOM 3092 C CB . HIS B 1 193 ? -8.998 21.533 12.195 1.00 21.97 ? 192 HIS B CB 1 ATOM 3093 C CG . HIS B 1 193 ? -7.496 21.533 12.245 1.00 27.20 ? 192 HIS B CG 1 ATOM 3094 N ND1 . HIS B 1 193 ? -6.787 21.233 13.387 1.00 20.50 ? 192 HIS B ND1 1 ATOM 3095 C CD2 . HIS B 1 193 ? -6.572 21.820 11.297 1.00 23.74 ? 192 HIS B CD2 1 ATOM 3096 C CE1 . HIS B 1 193 ? -5.497 21.344 13.141 1.00 19.98 ? 192 HIS B CE1 1 ATOM 3097 N NE2 . HIS B 1 193 ? -5.342 21.698 11.880 1.00 19.61 ? 192 HIS B NE2 1 ATOM 3098 N N . PRO B 1 194 ? -8.317 18.310 12.701 1.00 23.50 ? 193 PRO B N 1 ATOM 3099 C CA . PRO B 1 194 ? -8.056 17.289 13.738 1.00 22.12 ? 193 PRO B CA 1 ATOM 3100 C C . PRO B 1 194 ? -7.776 17.833 15.125 1.00 20.98 ? 193 PRO B C 1 ATOM 3101 O O . PRO B 1 194 ? -7.977 17.102 16.094 1.00 33.53 ? 193 PRO B O 1 ATOM 3102 C CB . PRO B 1 194 ? -6.854 16.511 13.184 1.00 19.47 ? 193 PRO B CB 1 ATOM 3103 C CG . PRO B 1 194 ? -6.361 17.304 11.987 1.00 21.87 ? 193 PRO B CG 1 ATOM 3104 C CD . PRO B 1 194 ? -7.530 18.078 11.478 1.00 17.29 ? 193 PRO B CD 1 ATOM 3105 N N . ALA B 1 195 ? -7.337 19.080 15.280 1.00 24.86 ? 194 ALA B N 1 ATOM 3106 C CA . ALA B 1 195 ? -7.110 19.608 16.623 1.00 21.67 ? 194 ALA B CA 1 ATOM 3107 C C . ALA B 1 195 ? -8.384 20.082 17.296 1.00 29.14 ? 194 ALA B C 1 ATOM 3108 O O . ALA B 1 195 ? -8.332 20.520 18.452 1.00 32.81 ? 194 ALA B O 1 ATOM 3109 C CB . ALA B 1 195 ? -6.114 20.762 16.594 1.00 20.56 ? 194 ALA B CB 1 ATOM 3110 N N . LEU B 1 196 ? -9.518 20.003 16.612 1.00 27.79 ? 195 LEU B N 1 ATOM 3111 C CA . LEU B 1 196 ? -10.775 20.515 17.127 1.00 25.70 ? 195 LEU B CA 1 ATOM 3112 C C . LEU B 1 196 ? -11.612 19.376 17.677 1.00 27.07 ? 195 LEU B C 1 ATOM 3113 O O . LEU B 1 196 ? -11.697 18.308 17.070 1.00 28.74 ? 195 LEU B O 1 ATOM 3114 C CB . LEU B 1 196 ? -11.537 21.258 16.032 1.00 23.53 ? 195 LEU B CB 1 ATOM 3115 C CG . LEU B 1 196 ? -10.844 22.514 15.500 1.00 29.55 ? 195 LEU B CG 1 ATOM 3116 C CD1 . LEU B 1 196 ? -11.589 23.101 14.309 1.00 27.05 ? 195 LEU B CD1 1 ATOM 3117 C CD2 . LEU B 1 196 ? -10.731 23.545 16.597 1.00 26.97 ? 195 LEU B CD2 1 ATOM 3118 N N . GLU B 1 197 ? -12.218 19.603 18.846 1.00 33.17 ? 196 GLU B N 1 ATOM 3119 C CA . GLU B 1 197 ? -13.154 18.626 19.393 1.00 31.66 ? 196 GLU B CA 1 ATOM 3120 C C . GLU B 1 197 ? -14.475 18.624 18.622 1.00 37.98 ? 196 GLU B C 1 ATOM 3121 O O . GLU B 1 197 ? -15.159 17.591 18.559 1.00 35.47 ? 196 GLU B O 1 ATOM 3122 C CB . GLU B 1 197 ? -13.377 18.917 20.871 1.00 34.81 ? 196 GLU B CB 1 ATOM 3123 C CG . GLU B 1 197 ? -12.079 18.893 21.658 1.00 48.96 ? 196 GLU B CG 1 ATOM 3124 C CD . GLU B 1 197 ? -12.265 18.390 23.077 1.00 54.95 ? 196 GLU B CD 1 ATOM 3125 O OE1 . GLU B 1 197 ? -12.204 19.222 24.009 1.00 57.19 ? 196 GLU B OE1 1 ATOM 3126 O OE2 . GLU B 1 197 ? -12.493 17.169 23.256 1.00 49.85 ? 196 GLU B OE2 1 ATOM 3127 N N A LYS B 1 198 ? -14.855 19.761 18.045 0.56 33.45 ? 197 LYS B N 1 ATOM 3128 N N B LYS B 1 198 ? -14.846 19.767 18.044 0.44 35.04 ? 197 LYS B N 1 ATOM 3129 C CA A LYS B 1 198 ? -15.967 19.796 17.110 0.56 34.91 ? 197 LYS B CA 1 ATOM 3130 C CA B LYS B 1 198 ? -16.009 19.897 17.177 0.44 34.86 ? 197 LYS B CA 1 ATOM 3131 C C A LYS B 1 198 ? -15.689 20.870 16.072 0.56 36.51 ? 197 LYS B C 1 ATOM 3132 C C B LYS B 1 198 ? -15.671 20.878 16.063 0.44 36.20 ? 197 LYS B C 1 ATOM 3133 O O A LYS B 1 198 ? -14.889 21.788 16.291 0.56 32.59 ? 197 LYS B O 1 ATOM 3134 O O B LYS B 1 198 ? -14.808 21.749 16.227 0.44 31.55 ? 197 LYS B O 1 ATOM 3135 C CB A LYS B 1 198 ? -17.318 20.040 17.808 0.56 32.98 ? 197 LYS B CB 1 ATOM 3136 C CB B LYS B 1 198 ? -17.254 20.392 17.940 0.44 32.81 ? 197 LYS B CB 1 ATOM 3137 C CG A LYS B 1 198 ? -17.519 21.433 18.396 0.56 30.91 ? 197 LYS B CG 1 ATOM 3138 C CG B LYS B 1 198 ? -18.430 19.421 17.956 0.44 33.14 ? 197 LYS B CG 1 ATOM 3139 C CD A LYS B 1 198 ? -18.949 21.596 18.917 0.56 30.71 ? 197 LYS B CD 1 ATOM 3140 C CD B LYS B 1 198 ? -19.759 20.126 17.664 0.44 34.31 ? 197 LYS B CD 1 ATOM 3141 C CE A LYS B 1 198 ? -19.275 23.046 19.295 0.56 32.93 ? 197 LYS B CE 1 ATOM 3142 C CE B LYS B 1 198 ? -20.982 19.227 17.929 0.44 32.41 ? 197 LYS B CE 1 ATOM 3143 N NZ A LYS B 1 198 ? -18.566 23.511 20.516 0.56 37.13 ? 197 LYS B NZ 1 ATOM 3144 N NZ B LYS B 1 198 ? -20.894 17.835 17.370 0.44 30.97 ? 197 LYS B NZ 1 ATOM 3145 N N . ASP B 1 199 ? -16.355 20.731 14.930 1.00 29.46 ? 198 ASP B N 1 ATOM 3146 C CA . ASP B 1 199 ? -16.196 21.692 13.850 1.00 31.19 ? 198 ASP B CA 1 ATOM 3147 C C . ASP B 1 199 ? -16.590 23.088 14.327 1.00 33.91 ? 198 ASP B C 1 ATOM 3148 O O . ASP B 1 199 ? -17.550 23.264 15.088 1.00 39.36 ? 198 ASP B O 1 ATOM 3149 C CB . ASP B 1 199 ? -17.044 21.299 12.624 1.00 28.56 ? 198 ASP B CB 1 ATOM 3150 C CG . ASP B 1 199 ? -16.675 19.933 12.043 1.00 36.34 ? 198 ASP B CG 1 ATOM 3151 O OD1 . ASP B 1 199 ? -15.651 19.334 12.447 1.00 42.38 ? 198 ASP B OD1 1 ATOM 3152 O OD2 . ASP B 1 199 ? -17.403 19.477 11.137 1.00 42.85 ? 198 ASP B OD2 1 ATOM 3153 N N . ILE B 1 200 ? -15.817 24.071 13.905 1.00 25.43 ? 199 ILE B N 1 ATOM 3154 C CA . ILE B 1 200 ? -16.171 25.465 14.096 1.00 27.51 ? 199 ILE B CA 1 ATOM 3155 C C . ILE B 1 200 ? -17.188 25.867 13.028 1.00 32.38 ? 199 ILE B C 1 ATOM 3156 O O . ILE B 1 200 ? -17.004 25.583 11.839 1.00 33.41 ? 199 ILE B O 1 ATOM 3157 C CB . ILE B 1 200 ? -14.911 26.337 14.037 1.00 23.66 ? 199 ILE B CB 1 ATOM 3158 C CG1 . ILE B 1 200 ? -13.993 26.001 15.215 1.00 25.67 ? 199 ILE B CG1 1 ATOM 3159 C CG2 . ILE B 1 200 ? -15.289 27.769 14.051 1.00 24.27 ? 199 ILE B CG2 1 ATOM 3160 C CD1 . ILE B 1 200 ? -12.666 26.769 15.214 1.00 21.44 ? 199 ILE B CD1 1 ATOM 3161 N N . ARG B 1 201 ? -18.284 26.501 13.447 1.00 31.30 ? 200 ARG B N 1 ATOM 3162 C CA . ARG B 1 201 ? -19.365 26.846 12.528 1.00 27.77 ? 200 ARG B CA 1 ATOM 3163 C C . ARG B 1 201 ? -19.768 28.288 12.762 1.00 32.08 ? 200 ARG B C 1 ATOM 3164 O O . ARG B 1 201 ? -20.151 28.653 13.876 1.00 32.94 ? 200 ARG B O 1 ATOM 3165 C CB . ARG B 1 201 ? -20.572 25.920 12.696 1.00 27.51 ? 200 ARG B CB 1 ATOM 3166 C CG . ARG B 1 201 ? -20.299 24.456 12.316 1.00 31.49 ? 200 ARG B CG 1 ATOM 3167 C CD . ARG B 1 201 ? -21.498 23.556 12.657 1.00 32.62 ? 200 ARG B CD 1 ATOM 3168 N NE . ARG B 1 201 ? -22.622 23.963 11.846 1.00 37.49 ? 200 ARG B NE 1 ATOM 3169 C CZ . ARG B 1 201 ? -22.993 23.347 10.735 1.00 33.48 ? 200 ARG B CZ 1 ATOM 3170 N NH1 . ARG B 1 201 ? -22.360 22.251 10.322 1.00 27.36 ? 200 ARG B NH1 1 ATOM 3171 N NH2 . ARG B 1 201 ? -24.014 23.832 10.049 1.00 40.55 ? 200 ARG B NH2 1 ATOM 3172 N N . TYR B 1 202 ? -19.660 29.103 11.720 1.00 33.55 ? 201 TYR B N 1 ATOM 3173 C CA . TYR B 1 202 ? -20.105 30.484 11.748 1.00 32.31 ? 201 TYR B CA 1 ATOM 3174 C C . TYR B 1 202 ? -21.043 30.744 10.586 1.00 33.25 ? 201 TYR B C 1 ATOM 3175 O O . TYR B 1 202 ? -20.828 30.257 9.475 1.00 33.09 ? 201 TYR B O 1 ATOM 3176 C CB . TYR B 1 202 ? -18.946 31.432 11.686 1.00 33.70 ? 201 TYR B CB 1 ATOM 3177 C CG . TYR B 1 202 ? -18.094 31.395 12.923 1.00 37.73 ? 201 TYR B CG 1 ATOM 3178 C CD1 . TYR B 1 202 ? -18.610 31.779 14.160 1.00 31.54 ? 201 TYR B CD1 1 ATOM 3179 C CD2 . TYR B 1 202 ? -16.762 30.979 12.853 1.00 32.98 ? 201 TYR B CD2 1 ATOM 3180 C CE1 . TYR B 1 202 ? -17.810 31.763 15.294 1.00 36.65 ? 201 TYR B CE1 1 ATOM 3181 C CE2 . TYR B 1 202 ? -15.960 30.965 13.969 1.00 28.63 ? 201 TYR B CE2 1 ATOM 3182 C CZ . TYR B 1 202 ? -16.477 31.351 15.180 1.00 38.32 ? 201 TYR B CZ 1 ATOM 3183 O OH . TYR B 1 202 ? -15.650 31.312 16.269 1.00 42.47 ? 201 TYR B OH 1 ATOM 3184 N N . SER B 1 203 ? -22.079 31.529 10.850 1.00 39.16 ? 202 SER B N 1 ATOM 3185 C CA . SER B 1 203 ? -23.114 31.770 9.865 1.00 34.43 ? 202 SER B CA 1 ATOM 3186 C C . SER B 1 203 ? -23.692 33.157 10.067 1.00 40.63 ? 202 SER B C 1 ATOM 3187 O O . SER B 1 203 ? -23.481 33.810 11.093 1.00 38.13 ? 202 SER B O 1 ATOM 3188 C CB . SER B 1 203 ? -24.228 30.732 9.966 1.00 44.75 ? 202 SER B CB 1 ATOM 3189 O OG . SER B 1 203 ? -24.822 30.785 11.251 1.00 45.89 ? 202 SER B OG 1 ATOM 3190 N N . PHE B 1 204 ? -24.437 33.598 9.063 1.00 49.04 ? 203 PHE B N 1 ATOM 3191 C CA . PHE B 1 204 ? -25.130 34.870 9.140 1.00 44.08 ? 203 PHE B CA 1 ATOM 3192 C C . PHE B 1 204 ? -26.150 34.922 8.015 1.00 48.51 ? 203 PHE B C 1 ATOM 3193 O O . PHE B 1 204 ? -26.105 34.129 7.065 1.00 45.05 ? 203 PHE B O 1 ATOM 3194 C CB . PHE B 1 204 ? -24.162 36.059 9.076 1.00 41.98 ? 203 PHE B CB 1 ATOM 3195 C CG . PHE B 1 204 ? -23.458 36.222 7.757 1.00 43.25 ? 203 PHE B CG 1 ATOM 3196 C CD1 . PHE B 1 204 ? -22.183 35.708 7.567 1.00 40.49 ? 203 PHE B CD1 1 ATOM 3197 C CD2 . PHE B 1 204 ? -24.054 36.925 6.719 1.00 46.68 ? 203 PHE B CD2 1 ATOM 3198 C CE1 . PHE B 1 204 ? -21.521 35.878 6.372 1.00 41.16 ? 203 PHE B CE1 1 ATOM 3199 C CE2 . PHE B 1 204 ? -23.407 37.095 5.515 1.00 45.80 ? 203 PHE B CE2 1 ATOM 3200 C CZ . PHE B 1 204 ? -22.134 36.572 5.341 1.00 51.82 ? 203 PHE B CZ 1 ATOM 3201 N N . ILE B 1 205 ? -27.078 35.865 8.145 1.00 53.53 ? 204 ILE B N 1 ATOM 3202 C CA . ILE B 1 205 ? -28.230 35.947 7.257 1.00 59.37 ? 204 ILE B CA 1 ATOM 3203 C C . ILE B 1 205 ? -27.908 36.895 6.106 1.00 60.26 ? 204 ILE B C 1 ATOM 3204 O O . ILE B 1 205 ? -27.359 37.989 6.312 1.00 49.20 ? 204 ILE B O 1 ATOM 3205 C CB . ILE B 1 205 ? -29.482 36.395 8.025 1.00 61.18 ? 204 ILE B CB 1 ATOM 3206 C CG1 . ILE B 1 205 ? -29.728 35.472 9.232 1.00 56.35 ? 204 ILE B CG1 1 ATOM 3207 C CG2 . ILE B 1 205 ? -30.691 36.416 7.101 1.00 59.43 ? 204 ILE B CG2 1 ATOM 3208 C CD1 . ILE B 1 205 ? -29.103 35.958 10.557 1.00 57.09 ? 204 ILE B CD1 1 ATOM 3209 N N . LEU B 1 206 ? -28.225 36.459 4.885 1.00 66.82 ? 205 LEU B N 1 ATOM 3210 C CA . LEU B 1 206 ? -27.915 37.237 3.690 1.00 67.33 ? 205 LEU B CA 1 ATOM 3211 C C . LEU B 1 206 ? -28.782 38.491 3.625 1.00 71.57 ? 205 LEU B C 1 ATOM 3212 O O . LEU B 1 206 ? -30.004 38.432 3.804 1.00 68.13 ? 205 LEU B O 1 ATOM 3213 C CB . LEU B 1 206 ? -28.132 36.386 2.436 1.00 68.10 ? 205 LEU B CB 1 ATOM 3214 C CG . LEU B 1 206 ? -27.132 35.273 2.112 1.00 65.77 ? 205 LEU B CG 1 ATOM 3215 C CD1 . LEU B 1 206 ? -27.512 34.565 0.808 1.00 57.25 ? 205 LEU B CD1 1 ATOM 3216 C CD2 . LEU B 1 206 ? -25.701 35.829 2.038 1.00 60.71 ? 205 LEU B CD2 1 ATOM 3217 N N . ASP B 1 207 ? -28.156 39.630 3.369 1.00 75.25 ? 206 ASP B N 1 ATOM 3218 C CA . ASP B 1 207 ? -28.880 40.876 3.159 1.00 68.96 ? 206 ASP B CA 1 ATOM 3219 C C . ASP B 1 207 ? -28.840 41.185 1.668 1.00 69.05 ? 206 ASP B C 1 ATOM 3220 O O . ASP B 1 207 ? -27.792 41.553 1.132 1.00 65.54 ? 206 ASP B O 1 ATOM 3221 C CB . ASP B 1 207 ? -28.281 42.010 3.985 1.00 65.86 ? 206 ASP B CB 1 ATOM 3222 C CG . ASP B 1 207 ? -29.235 43.187 4.130 1.00 83.87 ? 206 ASP B CG 1 ATOM 3223 O OD1 . ASP B 1 207 ? -30.171 43.299 3.306 1.00 79.03 ? 206 ASP B OD1 1 ATOM 3224 O OD2 . ASP B 1 207 ? -29.064 43.989 5.075 1.00 88.23 ? 206 ASP B OD2 1 ATOM 3225 N N . ILE B 1 208 ? -29.971 41.028 0.992 1.00 70.94 ? 207 ILE B N 1 ATOM 3226 C CA . ILE B 1 208 ? -30.082 41.356 -0.427 1.00 77.66 ? 207 ILE B CA 1 ATOM 3227 C C . ILE B 1 208 ? -30.996 42.575 -0.563 1.00 82.39 ? 207 ILE B C 1 ATOM 3228 O O . ILE B 1 208 ? -32.158 42.529 -0.145 1.00 87.74 ? 207 ILE B O 1 ATOM 3229 C CB . ILE B 1 208 ? -30.596 40.152 -1.230 1.00 70.45 ? 207 ILE B CB 1 ATOM 3230 C CG1 . ILE B 1 208 ? -29.791 38.910 -0.835 1.00 68.23 ? 207 ILE B CG1 1 ATOM 3231 C CG2 . ILE B 1 208 ? -30.448 40.403 -2.700 1.00 68.40 ? 207 ILE B CG2 1 ATOM 3232 C CD1 . ILE B 1 208 ? -29.965 37.745 -1.744 1.00 68.80 ? 207 ILE B CD1 1 ATOM 3233 N N . GLN B 1 209 ? -30.433 43.614 -1.161 1.00 80.04 ? 208 GLN B N 1 ATOM 3234 C CA . GLN B 1 209 ? -31.014 44.930 -1.305 1.00 89.02 ? 208 GLN B CA 1 ATOM 3235 C C . GLN B 1 209 ? -31.936 45.190 -2.496 1.00 91.23 ? 208 GLN B C 1 ATOM 3236 O O . GLN B 1 209 ? -32.244 44.318 -3.275 1.00 88.02 ? 208 GLN B O 1 ATOM 3237 C CB . GLN B 1 209 ? -29.880 45.926 -1.394 1.00 85.38 ? 208 GLN B CB 1 ATOM 3238 C CG . GLN B 1 209 ? -29.165 45.899 -2.731 1.00 89.05 ? 208 GLN B CG 1 ATOM 3239 C CD . GLN B 1 209 ? -29.000 44.501 -3.301 1.00 93.27 ? 208 GLN B CD 1 ATOM 3240 O OE1 . GLN B 1 209 ? -28.040 43.775 -2.969 1.00 92.78 ? 208 GLN B OE1 1 ATOM 3241 N NE2 . GLN B 1 209 ? -29.944 44.105 -4.162 1.00 93.28 ? 208 GLN B NE2 1 ATOM 3242 N N . HIS B 1 210 ? -32.313 46.457 -2.611 1.00 94.52 ? 209 HIS B N 1 ATOM 3243 C CA . HIS B 1 210 ? -33.306 47.008 -3.514 1.00 97.54 ? 209 HIS B CA 1 ATOM 3244 C C . HIS B 1 210 ? -32.631 47.490 -4.804 1.00 94.83 ? 209 HIS B C 1 ATOM 3245 O O . HIS B 1 210 ? -31.403 47.487 -4.930 1.00 92.62 ? 209 HIS B O 1 ATOM 3246 C CB . HIS B 1 210 ? -34.037 48.154 -2.800 1.00 99.86 ? 209 HIS B CB 1 ATOM 3247 C CG . HIS B 1 210 ? -34.248 47.908 -1.331 1.00 105.22 ? 209 HIS B CG 1 ATOM 3248 N ND1 . HIS B 1 210 ? -33.211 47.738 -0.436 1.00 100.85 ? 209 HIS B ND1 1 ATOM 3249 C CD2 . HIS B 1 210 ? -35.385 47.789 -0.606 1.00 107.91 ? 209 HIS B CD2 1 ATOM 3250 C CE1 . HIS B 1 210 ? -33.699 47.526 0.772 1.00 97.54 ? 209 HIS B CE1 1 ATOM 3251 N NE2 . HIS B 1 210 ? -35.016 47.556 0.697 1.00 107.12 ? 209 HIS B NE2 1 ATOM 3252 N N . HIS B 1 211 ? -33.292 47.824 -5.963 1.00 107.00 ? 210 HIS B N 1 ATOM 3253 C CA . HIS B 1 211 ? -32.849 48.250 -7.310 1.00 104.40 ? 210 HIS B CA 1 ATOM 3254 C C . HIS B 1 211 ? -31.808 47.313 -7.930 1.00 100.24 ? 210 HIS B C 1 ATOM 3255 O O . HIS B 1 211 ? -31.329 47.544 -9.046 1.00 101.73 ? 210 HIS B O 1 ATOM 3256 C CB . HIS B 1 211 ? -32.300 49.696 -7.298 1.00 103.30 ? 210 HIS B CB 1 ATOM 3257 C CG . HIS B 1 211 ? -30.838 49.815 -6.969 1.00 98.16 ? 210 HIS B CG 1 ATOM 3258 N ND1 . HIS B 1 211 ? -29.839 49.473 -7.857 1.00 101.28 ? 210 HIS B ND1 1 ATOM 3259 C CD2 . HIS B 1 211 ? -30.211 50.287 -5.866 1.00 92.46 ? 210 HIS B CD2 1 ATOM 3260 C CE1 . HIS B 1 211 ? -28.661 49.708 -7.307 1.00 94.53 ? 210 HIS B CE1 1 ATOM 3261 N NE2 . HIS B 1 211 ? -28.859 50.194 -6.095 1.00 95.29 ? 210 HIS B NE2 1 HETATM 3262 C C1 . NAG C 2 . ? 38.348 -29.933 16.298 1.00 34.92 ? 301 NAG A C1 1 HETATM 3263 C C2 . NAG C 2 . ? 38.435 -30.512 17.716 1.00 34.10 ? 301 NAG A C2 1 HETATM 3264 C C3 . NAG C 2 . ? 39.374 -31.709 17.761 1.00 40.04 ? 301 NAG A C3 1 HETATM 3265 C C4 . NAG C 2 . ? 38.922 -32.840 16.854 1.00 43.92 ? 301 NAG A C4 1 HETATM 3266 C C5 . NAG C 2 . ? 38.740 -32.353 15.417 1.00 41.40 ? 301 NAG A C5 1 HETATM 3267 C C6 . NAG C 2 . ? 37.792 -33.250 14.653 1.00 40.54 ? 301 NAG A C6 1 HETATM 3268 C C7 . NAG C 2 . ? 38.229 -28.620 19.292 1.00 38.07 ? 301 NAG A C7 1 HETATM 3269 C C8 . NAG C 2 . ? 39.005 -27.599 20.085 1.00 28.84 ? 301 NAG A C8 1 HETATM 3270 N N2 . NAG C 2 . ? 38.963 -29.477 18.585 1.00 36.40 ? 301 NAG A N2 1 HETATM 3271 O O3 . NAG C 2 . ? 39.464 -32.171 19.103 1.00 34.04 ? 301 NAG A O3 1 HETATM 3272 O O4 . NAG C 2 . ? 39.980 -33.799 16.806 1.00 43.80 ? 301 NAG A O4 1 HETATM 3273 O O5 . NAG C 2 . ? 38.169 -31.028 15.304 1.00 44.65 ? 301 NAG A O5 1 HETATM 3274 O O6 . NAG C 2 . ? 36.547 -33.350 15.336 1.00 61.11 ? 301 NAG A O6 1 HETATM 3275 O O7 . NAG C 2 . ? 37.007 -28.679 19.321 1.00 43.34 ? 301 NAG A O7 1 HETATM 3276 C C1 . NAG D 2 . ? 39.809 -35.088 17.452 1.00 45.36 ? 302 NAG A C1 1 HETATM 3277 C C2 . NAG D 2 . ? 40.869 -36.051 16.905 1.00 46.19 ? 302 NAG A C2 1 HETATM 3278 C C3 . NAG D 2 . ? 40.763 -37.413 17.589 1.00 54.53 ? 302 NAG A C3 1 HETATM 3279 C C4 . NAG D 2 . ? 40.487 -37.339 19.088 1.00 59.64 ? 302 NAG A C4 1 HETATM 3280 C C5 . NAG D 2 . ? 39.642 -36.137 19.520 1.00 52.32 ? 302 NAG A C5 1 HETATM 3281 C C6 . NAG D 2 . ? 39.793 -35.815 20.984 1.00 50.80 ? 302 NAG A C6 1 HETATM 3282 C C7 . NAG D 2 . ? 41.580 -35.769 14.575 1.00 47.05 ? 302 NAG A C7 1 HETATM 3283 C C8 . NAG D 2 . ? 41.229 -36.033 13.143 1.00 32.51 ? 302 NAG A C8 1 HETATM 3284 N N2 . NAG D 2 . ? 40.704 -36.214 15.474 1.00 51.26 ? 302 NAG A N2 1 HETATM 3285 O O3 . NAG D 2 . ? 41.960 -38.155 17.390 1.00 58.69 ? 302 NAG A O3 1 HETATM 3286 O O4 . NAG D 2 . ? 39.698 -38.500 19.337 1.00 86.56 ? 302 NAG A O4 1 HETATM 3287 O O5 . NAG D 2 . ? 39.993 -34.940 18.809 1.00 49.12 ? 302 NAG A O5 1 HETATM 3288 O O6 . NAG D 2 . ? 40.866 -34.905 21.179 1.00 66.73 ? 302 NAG A O6 1 HETATM 3289 O O7 . NAG D 2 . ? 42.613 -35.183 14.903 1.00 49.69 ? 302 NAG A O7 1 HETATM 3290 C C1 . BMA E 3 . ? 39.863 -39.156 20.613 1.00 84.84 ? 303 BMA A C1 1 HETATM 3291 C C2 . BMA E 3 . ? 38.501 -39.884 20.952 1.00 90.91 ? 303 BMA A C2 1 HETATM 3292 C C3 . BMA E 3 . ? 38.600 -40.552 22.326 1.00 91.96 ? 303 BMA A C3 1 HETATM 3293 C C4 . BMA E 3 . ? 39.928 -41.367 22.484 1.00 88.80 ? 303 BMA A C4 1 HETATM 3294 C C5 . BMA E 3 . ? 41.209 -40.586 21.972 1.00 83.60 ? 303 BMA A C5 1 HETATM 3295 C C6 . BMA E 3 . ? 42.436 -41.432 21.870 1.00 82.56 ? 303 BMA A C6 1 HETATM 3296 O O2 . BMA E 3 . ? 38.190 -40.884 19.983 1.00 98.35 ? 303 BMA A O2 1 HETATM 3297 O O3 . BMA E 3 . ? 37.456 -41.361 22.580 1.00 102.93 ? 303 BMA A O3 1 HETATM 3298 O O4 . BMA E 3 . ? 40.115 -41.666 23.869 1.00 81.46 ? 303 BMA A O4 1 HETATM 3299 O O5 . BMA E 3 . ? 41.002 -40.064 20.660 1.00 72.11 ? 303 BMA A O5 1 HETATM 3300 O O6 . BMA E 3 . ? 43.540 -40.559 22.021 1.00 81.60 ? 303 BMA A O6 1 HETATM 3301 C C1 . NAG F 2 . ? 3.664 29.737 12.302 1.00 29.36 ? 301 NAG B C1 1 HETATM 3302 C C2 . NAG F 2 . ? 3.225 30.416 13.623 1.00 28.49 ? 301 NAG B C2 1 HETATM 3303 C C3 . NAG F 2 . ? 2.220 31.534 13.365 1.00 28.51 ? 301 NAG B C3 1 HETATM 3304 C C4 . NAG F 2 . ? 2.747 32.523 12.340 1.00 27.02 ? 301 NAG B C4 1 HETATM 3305 C C5 . NAG F 2 . ? 3.028 31.758 11.060 1.00 30.23 ? 301 NAG B C5 1 HETATM 3306 C C6 . NAG F 2 . ? 3.563 32.635 9.954 1.00 32.17 ? 301 NAG B C6 1 HETATM 3307 C C7 . NAG F 2 . ? 3.307 28.984 15.607 1.00 35.95 ? 301 NAG B C7 1 HETATM 3308 C C8 . NAG F 2 . ? 2.525 28.072 16.504 1.00 20.43 ? 301 NAG B C8 1 HETATM 3309 N N2 . NAG F 2 . ? 2.647 29.470 14.556 1.00 26.40 ? 301 NAG B N2 1 HETATM 3310 O O3 . NAG F 2 . ? 1.928 32.178 14.599 1.00 29.41 ? 301 NAG B O3 1 HETATM 3311 O O4 . NAG F 2 . ? 1.739 33.486 12.068 1.00 35.03 ? 301 NAG B O4 1 HETATM 3312 O O5 . NAG F 2 . ? 4.019 30.752 11.316 1.00 35.26 ? 301 NAG B O5 1 HETATM 3313 O O6 . NAG F 2 . ? 4.383 33.673 10.470 1.00 34.02 ? 301 NAG B O6 1 HETATM 3314 O O7 . NAG F 2 . ? 4.499 29.235 15.801 1.00 40.23 ? 301 NAG B O7 1 HETATM 3315 C C1 . NAG G 2 . ? 2.012 34.821 12.492 1.00 34.85 ? 302 NAG B C1 1 HETATM 3316 C C2 . NAG G 2 . ? 0.985 35.685 11.742 1.00 38.42 ? 302 NAG B C2 1 HETATM 3317 C C3 . NAG G 2 . ? 1.071 37.144 12.189 1.00 42.45 ? 302 NAG B C3 1 HETATM 3318 C C4 . NAG G 2 . ? 0.919 37.240 13.698 1.00 39.70 ? 302 NAG B C4 1 HETATM 3319 C C5 . NAG G 2 . ? 2.001 36.385 14.351 1.00 44.94 ? 302 NAG B C5 1 HETATM 3320 C C6 . NAG G 2 . ? 1.886 36.351 15.852 1.00 44.16 ? 302 NAG B C6 1 HETATM 3321 C C7 . NAG G 2 . ? 0.248 35.051 9.481 1.00 39.45 ? 302 NAG B C7 1 HETATM 3322 C C8 . NAG G 2 . ? -1.013 34.557 10.128 1.00 29.93 ? 302 NAG B C8 1 HETATM 3323 N N2 . NAG G 2 . ? 1.165 35.583 10.302 1.00 34.99 ? 302 NAG B N2 1 HETATM 3324 O O3 . NAG G 2 . ? 0.046 37.892 11.547 1.00 45.54 ? 302 NAG B O3 1 HETATM 3325 O O4 . NAG G 2 . ? 1.037 38.602 14.095 1.00 53.81 ? 302 NAG B O4 1 HETATM 3326 O O5 . NAG G 2 . ? 1.878 35.021 13.905 1.00 40.58 ? 302 NAG B O5 1 HETATM 3327 O O6 . NAG G 2 . ? 0.539 36.105 16.227 1.00 47.79 ? 302 NAG B O6 1 HETATM 3328 O O7 . NAG G 2 . ? 0.423 34.981 8.270 1.00 37.25 ? 302 NAG B O7 1 HETATM 3329 C C1 . BMA H 3 . ? -0.045 39.078 14.945 1.00 52.50 ? 303 BMA B C1 1 HETATM 3330 C C2 . BMA H 3 . ? 0.471 40.309 15.759 1.00 54.48 ? 303 BMA B C2 1 HETATM 3331 C C3 . BMA H 3 . ? -0.711 41.103 16.202 1.00 62.30 ? 303 BMA B C3 1 HETATM 3332 C C4 . BMA H 3 . ? -1.342 41.806 15.006 1.00 66.20 ? 303 BMA B C4 1 HETATM 3333 C C5 . BMA H 3 . ? -1.543 40.812 13.815 1.00 62.94 ? 303 BMA B C5 1 HETATM 3334 C C6 . BMA H 3 . ? -0.772 41.176 12.528 1.00 62.35 ? 303 BMA B C6 1 HETATM 3335 O O2 . BMA H 3 . ? 1.281 41.181 14.980 1.00 58.85 ? 303 BMA B O2 1 HETATM 3336 O O3 . BMA H 3 . ? -0.349 42.035 17.210 1.00 56.94 ? 303 BMA B O3 1 HETATM 3337 O O4 . BMA H 3 . ? -2.607 42.338 15.399 1.00 74.70 ? 303 BMA B O4 1 HETATM 3338 O O5 . BMA H 3 . ? -1.256 39.408 14.199 1.00 64.49 ? 303 BMA B O5 1 HETATM 3339 O O6 . BMA H 3 . ? -1.506 42.164 11.781 1.00 49.32 ? 303 BMA B O6 1 HETATM 3340 O O . HOH I 4 . ? 36.349 8.117 24.942 1.00 69.16 ? 401 HOH A O 1 HETATM 3341 O O . HOH I 4 . ? 37.220 -18.799 11.383 1.00 40.56 ? 402 HOH A O 1 HETATM 3342 O O . HOH I 4 . ? 68.392 -41.116 15.273 1.00 83.09 ? 403 HOH A O 1 HETATM 3343 O O . HOH I 4 . ? 63.114 -42.890 9.143 1.00 63.61 ? 404 HOH A O 1 HETATM 3344 O O . HOH I 4 . ? 71.557 -31.278 12.301 1.00 61.65 ? 405 HOH A O 1 HETATM 3345 O O . HOH I 4 . ? 34.891 5.674 31.948 1.00 64.85 ? 406 HOH A O 1 HETATM 3346 O O . HOH I 4 . ? 43.968 -33.201 17.555 1.00 42.01 ? 407 HOH A O 1 HETATM 3347 O O . HOH I 4 . ? 58.478 -39.405 19.047 1.00 55.97 ? 408 HOH A O 1 HETATM 3348 O O . HOH I 4 . ? 30.755 4.893 40.529 1.00 54.11 ? 409 HOH A O 1 HETATM 3349 O O . HOH I 4 . ? 74.930 -50.509 7.569 1.00 59.72 ? 410 HOH A O 1 HETATM 3350 O O . HOH I 4 . ? 71.834 -41.955 0.846 1.00 77.62 ? 411 HOH A O 1 HETATM 3351 O O . HOH I 4 . ? 35.146 -22.280 34.374 1.00 26.81 ? 412 HOH A O 1 HETATM 3352 O O . HOH I 4 . ? 68.095 -46.989 10.969 1.00 83.33 ? 413 HOH A O 1 HETATM 3353 O O . HOH I 4 . ? 21.477 -2.433 50.396 1.00 54.65 ? 414 HOH A O 1 HETATM 3354 O O . HOH I 4 . ? 23.877 -1.768 48.869 1.00 56.03 ? 415 HOH A O 1 HETATM 3355 O O . HOH I 4 . ? 39.543 -10.074 18.391 1.00 48.56 ? 416 HOH A O 1 HETATM 3356 O O . HOH I 4 . ? 62.647 -20.635 16.486 1.00 40.71 ? 417 HOH A O 1 HETATM 3357 O O . HOH I 4 . ? 41.644 -18.332 13.745 1.00 37.48 ? 418 HOH A O 1 HETATM 3358 O O . HOH I 4 . ? 54.608 -17.203 9.002 1.00 38.91 ? 419 HOH A O 1 HETATM 3359 O O . HOH I 4 . ? 58.106 -48.543 3.533 1.00 63.25 ? 420 HOH A O 1 HETATM 3360 O O . HOH I 4 . ? 40.995 -22.050 32.150 1.00 35.84 ? 421 HOH A O 1 HETATM 3361 O O . HOH I 4 . ? 22.396 -3.361 31.683 1.00 25.08 ? 422 HOH A O 1 HETATM 3362 O O . HOH I 4 . ? 43.803 -17.225 26.142 1.00 29.67 ? 423 HOH A O 1 HETATM 3363 O O . HOH I 4 . ? 50.821 -24.406 7.127 1.00 28.05 ? 424 HOH A O 1 HETATM 3364 O O . HOH I 4 . ? 22.373 10.755 41.307 1.00 28.73 ? 425 HOH A O 1 HETATM 3365 O O . HOH I 4 . ? 22.411 -6.181 30.582 1.00 37.51 ? 426 HOH A O 1 HETATM 3366 O O . HOH I 4 . ? 38.140 -26.036 28.490 1.00 33.00 ? 427 HOH A O 1 HETATM 3367 O O . HOH I 4 . ? 45.255 -29.316 19.354 1.00 27.26 ? 428 HOH A O 1 HETATM 3368 O O . HOH I 4 . ? 34.983 -28.435 21.121 1.00 34.75 ? 429 HOH A O 1 HETATM 3369 O O . HOH I 4 . ? 69.461 -25.517 9.190 1.00 66.44 ? 430 HOH A O 1 HETATM 3370 O O . HOH I 4 . ? 29.378 9.148 27.878 1.00 49.95 ? 431 HOH A O 1 HETATM 3371 O O . HOH I 4 . ? 34.632 8.801 23.296 1.00 59.83 ? 432 HOH A O 1 HETATM 3372 O O . HOH I 4 . ? 41.696 -29.081 18.985 1.00 34.81 ? 433 HOH A O 1 HETATM 3373 O O . HOH I 4 . ? 60.060 -36.941 19.610 1.00 53.90 ? 434 HOH A O 1 HETATM 3374 O O . HOH I 4 . ? 50.453 -34.495 17.301 1.00 41.10 ? 435 HOH A O 1 HETATM 3375 O O . HOH I 4 . ? 41.887 -9.339 35.096 1.00 35.59 ? 436 HOH A O 1 HETATM 3376 O O . HOH I 4 . ? 48.050 -27.052 12.595 1.00 31.08 ? 437 HOH A O 1 HETATM 3377 O O . HOH I 4 . ? 41.459 -22.260 10.516 1.00 38.81 ? 438 HOH A O 1 HETATM 3378 O O . HOH I 4 . ? 29.534 -18.437 24.541 1.00 33.35 ? 439 HOH A O 1 HETATM 3379 O O . HOH I 4 . ? 35.687 -0.084 20.675 1.00 38.91 ? 440 HOH A O 1 HETATM 3380 O O . HOH I 4 . ? 41.205 -29.161 3.712 1.00 50.48 ? 441 HOH A O 1 HETATM 3381 O O . HOH I 4 . ? 40.968 -21.118 34.598 1.00 38.81 ? 442 HOH A O 1 HETATM 3382 O O . HOH I 4 . ? 50.162 -28.816 3.040 1.00 56.53 ? 443 HOH A O 1 HETATM 3383 O O . HOH I 4 . ? 21.915 7.554 26.730 1.00 51.97 ? 444 HOH A O 1 HETATM 3384 O O . HOH I 4 . ? 36.743 -25.307 26.214 1.00 34.30 ? 445 HOH A O 1 HETATM 3385 O O . HOH I 4 . ? 39.023 -11.946 37.580 1.00 39.95 ? 446 HOH A O 1 HETATM 3386 O O . HOH I 4 . ? 38.388 -17.195 12.892 1.00 45.30 ? 447 HOH A O 1 HETATM 3387 O O . HOH I 4 . ? 27.754 -22.791 31.154 1.00 37.63 ? 448 HOH A O 1 HETATM 3388 O O . HOH I 4 . ? 59.807 -25.714 22.445 1.00 48.14 ? 449 HOH A O 1 HETATM 3389 O O . HOH I 4 . ? 37.500 -16.918 16.081 1.00 40.49 ? 450 HOH A O 1 HETATM 3390 O O . HOH I 4 . ? 21.293 -20.731 31.999 1.00 35.25 ? 451 HOH A O 1 HETATM 3391 O O . HOH I 4 . ? 42.405 -19.975 36.070 1.00 39.25 ? 452 HOH A O 1 HETATM 3392 O O . HOH I 4 . ? 63.569 -32.634 21.661 1.00 46.39 ? 453 HOH A O 1 HETATM 3393 O O . HOH I 4 . ? 27.799 -16.762 23.183 1.00 46.25 ? 454 HOH A O 1 HETATM 3394 O O . HOH I 4 . ? 22.555 12.175 39.356 1.00 54.45 ? 455 HOH A O 1 HETATM 3395 O O . HOH I 4 . ? 48.937 -30.380 1.299 1.00 56.49 ? 456 HOH A O 1 HETATM 3396 O O . HOH I 4 . ? 40.938 -5.461 41.904 1.00 57.75 ? 457 HOH A O 1 HETATM 3397 O O . HOH I 4 . ? 30.683 15.332 38.529 1.00 46.67 ? 458 HOH A O 1 HETATM 3398 O O . HOH I 4 . ? 55.510 -16.551 11.035 1.00 33.62 ? 459 HOH A O 1 HETATM 3399 O O . HOH I 4 . ? 59.412 -40.519 -4.393 1.00 91.44 ? 460 HOH A O 1 HETATM 3400 O O . HOH I 4 . ? 38.190 6.066 33.305 1.00 49.11 ? 461 HOH A O 1 HETATM 3401 O O . HOH I 4 . ? 43.362 -23.385 32.493 1.00 42.77 ? 462 HOH A O 1 HETATM 3402 O O . HOH I 4 . ? 76.491 -49.006 14.844 1.00 64.10 ? 463 HOH A O 1 HETATM 3403 O O . HOH I 4 . ? 38.492 -0.956 15.872 1.00 49.37 ? 464 HOH A O 1 HETATM 3404 O O . HOH I 4 . ? 42.353 -29.473 21.406 1.00 31.32 ? 465 HOH A O 1 HETATM 3405 O O . HOH I 4 . ? 28.871 11.330 28.183 1.00 47.54 ? 466 HOH A O 1 HETATM 3406 O O . HOH I 4 . ? 25.814 -1.204 49.991 1.00 41.19 ? 467 HOH A O 1 HETATM 3407 O O . HOH I 4 . ? 47.723 -35.782 16.489 1.00 48.76 ? 468 HOH A O 1 HETATM 3408 O O . HOH I 4 . ? 37.540 -0.231 18.047 1.00 64.32 ? 469 HOH A O 1 HETATM 3409 O O . HOH I 4 . ? 29.043 16.792 39.743 1.00 46.20 ? 470 HOH A O 1 HETATM 3410 O O . HOH I 4 . ? 41.499 3.559 37.622 1.00 40.01 ? 471 HOH A O 1 HETATM 3411 O O . HOH I 4 . ? 43.289 -0.474 43.672 1.00 54.95 ? 472 HOH A O 1 HETATM 3412 O O . HOH J 4 . ? -31.328 43.548 -4.652 1.00 77.54 ? 401 HOH B O 1 HETATM 3413 O O . HOH J 4 . ? 16.991 -10.238 33.784 1.00 51.01 ? 402 HOH B O 1 HETATM 3414 O O . HOH J 4 . ? -33.682 38.220 -8.688 1.00 51.27 ? 403 HOH B O 1 HETATM 3415 O O . HOH J 4 . ? 8.916 -6.758 36.929 1.00 46.31 ? 404 HOH B O 1 HETATM 3416 O O . HOH J 4 . ? -18.438 40.925 -2.361 1.00 54.72 ? 405 HOH B O 1 HETATM 3417 O O . HOH J 4 . ? 1.429 13.436 34.220 1.00 33.86 ? 406 HOH B O 1 HETATM 3418 O O . HOH J 4 . ? -1.310 26.816 26.128 1.00 38.68 ? 407 HOH B O 1 HETATM 3419 O O . HOH J 4 . ? 23.802 5.290 45.394 1.00 41.16 ? 408 HOH B O 1 HETATM 3420 O O . HOH J 4 . ? -24.076 43.499 -9.656 1.00 57.74 ? 409 HOH B O 1 HETATM 3421 O O . HOH J 4 . ? 10.163 -11.634 33.369 1.00 57.73 ? 410 HOH B O 1 HETATM 3422 O O . HOH J 4 . ? 5.810 30.103 10.024 1.00 30.51 ? 411 HOH B O 1 HETATM 3423 O O . HOH J 4 . ? -4.574 2.967 26.599 1.00 58.12 ? 412 HOH B O 1 HETATM 3424 O O . HOH J 4 . ? 5.395 -7.927 22.517 1.00 38.84 ? 413 HOH B O 1 HETATM 3425 O O . HOH J 4 . ? -1.542 44.378 10.872 1.00 50.52 ? 414 HOH B O 1 HETATM 3426 O O . HOH J 4 . ? -4.777 14.733 19.416 1.00 40.04 ? 415 HOH B O 1 HETATM 3427 O O . HOH J 4 . ? -28.290 38.442 -9.585 1.00 52.91 ? 416 HOH B O 1 HETATM 3428 O O . HOH J 4 . ? -15.319 21.379 6.824 1.00 31.52 ? 417 HOH B O 1 HETATM 3429 O O . HOH J 4 . ? 6.735 -6.279 34.887 1.00 48.26 ? 418 HOH B O 1 HETATM 3430 O O . HOH J 4 . ? 4.209 -7.712 35.803 1.00 49.61 ? 419 HOH B O 1 HETATM 3431 O O . HOH J 4 . ? -25.795 31.896 -6.761 1.00 59.04 ? 420 HOH B O 1 HETATM 3432 O O . HOH J 4 . ? -10.473 30.158 15.653 1.00 36.24 ? 421 HOH B O 1 HETATM 3433 O O . HOH J 4 . ? 2.600 5.983 24.623 1.00 32.37 ? 422 HOH B O 1 HETATM 3434 O O . HOH J 4 . ? -2.686 17.797 22.634 1.00 25.84 ? 423 HOH B O 1 HETATM 3435 O O . HOH J 4 . ? 11.130 17.422 16.371 1.00 38.24 ? 424 HOH B O 1 HETATM 3436 O O . HOH J 4 . ? -14.326 23.360 18.226 1.00 30.04 ? 425 HOH B O 1 HETATM 3437 O O . HOH J 4 . ? -5.937 26.019 8.256 1.00 20.48 ? 426 HOH B O 1 HETATM 3438 O O . HOH J 4 . ? -4.153 29.493 14.560 1.00 25.72 ? 427 HOH B O 1 HETATM 3439 O O . HOH J 4 . ? 5.805 12.699 46.920 1.00 38.08 ? 428 HOH B O 1 HETATM 3440 O O . HOH J 4 . ? 7.159 5.974 37.628 1.00 33.15 ? 429 HOH B O 1 HETATM 3441 O O . HOH J 4 . ? -8.886 35.889 -1.221 1.00 55.76 ? 430 HOH B O 1 HETATM 3442 O O . HOH J 4 . ? -25.883 27.394 10.613 1.00 48.58 ? 431 HOH B O 1 HETATM 3443 O O . HOH J 4 . ? 20.572 16.254 35.400 1.00 32.92 ? 432 HOH B O 1 HETATM 3444 O O . HOH J 4 . ? -2.516 33.868 7.721 1.00 20.61 ? 433 HOH B O 1 HETATM 3445 O O . HOH J 4 . ? -7.933 22.495 3.022 1.00 24.60 ? 434 HOH B O 1 HETATM 3446 O O . HOH J 4 . ? 1.914 10.599 14.980 1.00 35.24 ? 435 HOH B O 1 HETATM 3447 O O . HOH J 4 . ? -0.270 23.072 28.690 1.00 32.05 ? 436 HOH B O 1 HETATM 3448 O O . HOH J 4 . ? -21.621 41.551 1.009 1.00 53.46 ? 437 HOH B O 1 HETATM 3449 O O . HOH J 4 . ? -18.016 18.641 14.657 1.00 34.00 ? 438 HOH B O 1 HETATM 3450 O O . HOH J 4 . ? -1.517 21.339 5.596 1.00 30.02 ? 439 HOH B O 1 HETATM 3451 O O . HOH J 4 . ? -3.421 8.084 31.940 1.00 40.92 ? 440 HOH B O 1 HETATM 3452 O O . HOH J 4 . ? -28.359 22.547 -4.223 1.00 63.85 ? 441 HOH B O 1 HETATM 3453 O O . HOH J 4 . ? -14.396 15.498 20.101 1.00 32.20 ? 442 HOH B O 1 HETATM 3454 O O . HOH J 4 . ? -27.833 20.465 0.059 1.00 43.34 ? 443 HOH B O 1 HETATM 3455 O O . HOH J 4 . ? 17.385 4.141 31.205 1.00 28.60 ? 444 HOH B O 1 HETATM 3456 O O . HOH J 4 . ? 4.206 7.278 35.727 1.00 29.53 ? 445 HOH B O 1 HETATM 3457 O O . HOH J 4 . ? -7.103 26.523 -1.249 1.00 30.04 ? 446 HOH B O 1 HETATM 3458 O O . HOH J 4 . ? -4.550 40.433 14.988 1.00 66.38 ? 447 HOH B O 1 HETATM 3459 O O . HOH J 4 . ? 16.370 -9.344 41.654 1.00 34.37 ? 448 HOH B O 1 HETATM 3460 O O . HOH J 4 . ? -26.575 27.764 6.394 1.00 36.04 ? 449 HOH B O 1 HETATM 3461 O O . HOH J 4 . ? -5.909 23.511 1.622 1.00 28.40 ? 450 HOH B O 1 HETATM 3462 O O . HOH J 4 . ? -0.923 34.442 0.953 1.00 43.07 ? 451 HOH B O 1 HETATM 3463 O O . HOH J 4 . ? 3.788 20.422 6.058 1.00 63.06 ? 452 HOH B O 1 HETATM 3464 O O . HOH J 4 . ? -3.182 25.064 18.736 1.00 26.66 ? 453 HOH B O 1 HETATM 3465 O O . HOH J 4 . ? -9.118 34.413 11.263 1.00 29.60 ? 454 HOH B O 1 HETATM 3466 O O . HOH J 4 . ? 4.362 36.263 9.440 1.00 45.05 ? 455 HOH B O 1 HETATM 3467 O O . HOH J 4 . ? -0.407 29.065 14.432 1.00 25.20 ? 456 HOH B O 1 HETATM 3468 O O . HOH J 4 . ? 0.501 17.940 10.597 1.00 28.80 ? 457 HOH B O 1 HETATM 3469 O O . HOH J 4 . ? -2.541 33.487 12.607 1.00 35.52 ? 458 HOH B O 1 HETATM 3470 O O . HOH J 4 . ? -11.870 22.134 20.067 1.00 38.98 ? 459 HOH B O 1 HETATM 3471 O O . HOH J 4 . ? -10.920 22.808 2.620 1.00 33.55 ? 460 HOH B O 1 HETATM 3472 O O . HOH J 4 . ? 9.307 0.166 18.583 1.00 40.48 ? 461 HOH B O 1 HETATM 3473 O O . HOH J 4 . ? -2.780 3.146 24.615 1.00 53.11 ? 462 HOH B O 1 HETATM 3474 O O . HOH J 4 . ? -1.276 5.157 31.625 1.00 33.01 ? 463 HOH B O 1 HETATM 3475 O O . HOH J 4 . ? 6.924 30.045 13.999 1.00 37.23 ? 464 HOH B O 1 HETATM 3476 O O . HOH J 4 . ? -18.526 26.758 16.290 1.00 21.95 ? 465 HOH B O 1 HETATM 3477 O O . HOH J 4 . ? -23.496 29.815 13.610 1.00 37.90 ? 466 HOH B O 1 HETATM 3478 O O . HOH J 4 . ? 5.862 0.846 18.832 1.00 35.83 ? 467 HOH B O 1 HETATM 3479 O O . HOH J 4 . ? -1.917 6.235 39.830 1.00 39.06 ? 468 HOH B O 1 HETATM 3480 O O . HOH J 4 . ? 9.399 12.812 45.951 1.00 42.31 ? 469 HOH B O 1 HETATM 3481 O O . HOH J 4 . ? 2.518 6.225 10.867 1.00 53.92 ? 470 HOH B O 1 HETATM 3482 O O . HOH J 4 . ? 4.274 33.696 15.495 1.00 35.37 ? 471 HOH B O 1 HETATM 3483 O O . HOH J 4 . ? -4.439 19.094 26.733 1.00 31.74 ? 472 HOH B O 1 HETATM 3484 O O . HOH J 4 . ? -31.161 25.836 -0.875 1.00 74.60 ? 473 HOH B O 1 HETATM 3485 O O . HOH J 4 . ? 6.666 4.570 16.628 1.00 42.25 ? 474 HOH B O 1 HETATM 3486 O O . HOH J 4 . ? 6.720 25.912 19.261 1.00 20.69 ? 475 HOH B O 1 HETATM 3487 O O . HOH J 4 . ? -23.078 25.228 -0.559 1.00 58.39 ? 476 HOH B O 1 HETATM 3488 O O . HOH J 4 . ? 0.515 7.677 24.430 1.00 24.19 ? 477 HOH B O 1 HETATM 3489 O O . HOH J 4 . ? 12.915 12.421 16.024 1.00 37.57 ? 478 HOH B O 1 HETATM 3490 O O . HOH J 4 . ? -38.064 43.052 -3.216 1.00 59.88 ? 479 HOH B O 1 HETATM 3491 O O . HOH J 4 . ? -11.110 26.547 -5.023 1.00 42.35 ? 480 HOH B O 1 HETATM 3492 O O . HOH J 4 . ? 6.061 19.738 14.685 1.00 25.77 ? 481 HOH B O 1 HETATM 3493 O O . HOH J 4 . ? 4.806 17.346 13.787 1.00 26.89 ? 482 HOH B O 1 HETATM 3494 O O . HOH J 4 . ? 21.018 1.139 41.170 1.00 32.65 ? 483 HOH B O 1 HETATM 3495 O O . HOH J 4 . ? -12.963 18.016 13.683 1.00 38.28 ? 484 HOH B O 1 HETATM 3496 O O . HOH J 4 . ? 18.141 7.597 30.099 1.00 39.72 ? 485 HOH B O 1 HETATM 3497 O O . HOH J 4 . ? -1.078 33.027 14.642 1.00 39.02 ? 486 HOH B O 1 HETATM 3498 O O . HOH J 4 . ? -9.477 32.194 -3.650 1.00 34.87 ? 487 HOH B O 1 HETATM 3499 O O . HOH J 4 . ? -22.738 32.062 13.914 1.00 41.29 ? 488 HOH B O 1 HETATM 3500 O O . HOH J 4 . ? -6.794 25.708 -3.516 1.00 34.66 ? 489 HOH B O 1 HETATM 3501 O O . HOH J 4 . ? 19.102 11.800 43.110 1.00 47.87 ? 490 HOH B O 1 HETATM 3502 O O . HOH J 4 . ? 9.378 24.570 19.316 1.00 28.19 ? 491 HOH B O 1 HETATM 3503 O O . HOH J 4 . ? -9.566 33.220 -1.661 1.00 38.27 ? 492 HOH B O 1 HETATM 3504 O O . HOH J 4 . ? 12.456 15.112 15.540 1.00 40.41 ? 493 HOH B O 1 HETATM 3505 O O . HOH J 4 . ? 9.937 12.200 43.436 1.00 40.92 ? 494 HOH B O 1 HETATM 3506 O O . HOH J 4 . ? -8.630 24.837 -4.360 1.00 45.39 ? 495 HOH B O 1 HETATM 3507 O O . HOH J 4 . ? 11.040 1.035 16.631 1.00 49.06 ? 496 HOH B O 1 HETATM 3508 O O . HOH J 4 . ? -3.511 33.843 15.925 1.00 48.00 ? 497 HOH B O 1 HETATM 3509 O O . HOH J 4 . ? 13.778 -7.432 29.415 1.00 38.18 ? 498 HOH B O 1 HETATM 3510 O O . HOH J 4 . ? -17.207 28.380 17.783 1.00 35.84 ? 499 HOH B O 1 HETATM 3511 O O . HOH J 4 . ? -38.659 35.062 -1.119 1.00 49.47 ? 500 HOH B O 1 HETATM 3512 O O . HOH J 4 . ? 5.168 11.046 48.211 1.00 37.44 ? 501 HOH B O 1 HETATM 3513 O O . HOH J 4 . ? 10.497 14.855 13.638 1.00 49.10 ? 502 HOH B O 1 HETATM 3514 O O . HOH J 4 . ? 1.324 18.531 8.084 1.00 31.68 ? 503 HOH B O 1 HETATM 3515 O O . HOH J 4 . ? -4.441 35.107 8.294 1.00 41.77 ? 504 HOH B O 1 HETATM 3516 O O . HOH J 4 . ? 22.838 16.608 34.172 1.00 40.72 ? 505 HOH B O 1 HETATM 3517 O O . HOH J 4 . ? 24.043 6.385 47.732 1.00 40.03 ? 506 HOH B O 1 HETATM 3518 O O . HOH J 4 . ? 20.222 16.914 37.970 1.00 43.11 ? 507 HOH B O 1 HETATM 3519 O O . HOH J 4 . ? 1.956 4.101 9.134 1.00 82.07 ? 508 HOH B O 1 HETATM 3520 O O . HOH J 4 . ? 21.804 15.371 37.737 1.00 54.35 ? 509 HOH B O 1 HETATM 3521 O O . HOH J 4 . ? -39.897 34.691 0.997 1.00 42.90 ? 510 HOH B O 1 HETATM 3522 O O . HOH J 4 . ? 24.064 6.454 50.154 1.00 41.66 ? 511 HOH B O 1 # loop_ _atom_site_anisotrop.id _atom_site_anisotrop.type_symbol _atom_site_anisotrop.pdbx_label_atom_id _atom_site_anisotrop.pdbx_label_alt_id _atom_site_anisotrop.pdbx_label_comp_id _atom_site_anisotrop.pdbx_label_asym_id _atom_site_anisotrop.pdbx_label_seq_id _atom_site_anisotrop.pdbx_PDB_ins_code _atom_site_anisotrop.U[1][1] _atom_site_anisotrop.U[2][2] _atom_site_anisotrop.U[3][3] _atom_site_anisotrop.U[1][2] _atom_site_anisotrop.U[1][3] _atom_site_anisotrop.U[2][3] _atom_site_anisotrop.pdbx_auth_seq_id _atom_site_anisotrop.pdbx_auth_comp_id _atom_site_anisotrop.pdbx_auth_asym_id _atom_site_anisotrop.pdbx_auth_atom_id 1 N N . PRO A 1 ? 0.7482 0.7138 0.7515 -0.0103 -0.0470 -0.0081 0 PRO A N 2 C CA . PRO A 1 ? 0.9419 0.8991 0.9382 -0.0079 -0.0502 -0.0051 0 PRO A CA 3 C C . PRO A 1 ? 0.9583 0.9049 0.9514 -0.0059 -0.0535 -0.0041 0 PRO A C 4 O O . PRO A 1 ? 0.9476 0.8944 0.9432 -0.0075 -0.0560 -0.0036 0 PRO A O 5 C CB . PRO A 1 ? 0.7520 0.7070 0.7446 -0.0055 -0.0474 -0.0056 0 PRO A CB 6 C CG . PRO A 1 ? 0.8654 0.8317 0.8635 -0.0078 -0.0431 -0.0080 0 PRO A CG 7 C CD . PRO A 1 ? 0.7648 0.7382 0.7699 -0.0110 -0.0430 -0.0096 0 PRO A CD 8 N N . SER A 2 ? 0.9067 0.8441 0.8943 -0.0026 -0.0536 -0.0037 1 SER A N 9 C CA . SER A 2 ? 0.9633 0.8903 0.9478 -0.0005 -0.0562 -0.0030 1 SER A CA 10 C C . SER A 2 ? 0.9553 0.8812 0.9427 0.0001 -0.0538 -0.0058 1 SER A C 11 O O . SER A 2 ? 0.7847 0.7064 0.7695 0.0025 -0.0536 -0.0051 1 SER A O 12 C CB . SER A 2 ? 0.9693 0.8876 0.9461 0.0027 -0.0574 -0.0010 1 SER A CB 13 O OG . SER A 2 ? 1.1281 1.0472 1.1031 0.0039 -0.0545 -0.0017 1 SER A OG 14 N N . ILE A 3 ? 0.9423 0.8773 0.9357 -0.0018 -0.0501 -0.0084 2 ILE A N 15 C CA . ILE A 3 ? 0.8858 0.8208 0.8825 -0.0014 -0.0473 -0.0113 2 ILE A CA 16 C C . ILE A 3 ? 0.7131 0.6528 0.7159 -0.0041 -0.0480 -0.0121 2 ILE A C 17 O O . ILE A 3 ? 0.8019 0.7513 0.8098 -0.0072 -0.0469 -0.0127 2 ILE A O 18 C CB . ILE A 3 ? 0.8457 0.7875 0.8448 -0.0016 -0.0424 -0.0137 2 ILE A CB 19 C CG1 . ILE A 3 ? 0.7426 0.6825 0.7364 0.0002 -0.0418 -0.0124 2 ILE A CG1 20 C CG2 . ILE A 3 ? 0.7898 0.7287 0.7903 0.0001 -0.0395 -0.0163 2 ILE A CG2 21 C CD1 . ILE A 3 ? 0.6469 0.5751 0.6338 0.0042 -0.0429 -0.0113 2 ILE A CD1 22 N N . ILE A 4 ? 0.6331 0.5678 0.6357 -0.0028 -0.0490 -0.0117 3 ILE A N 23 C CA . ILE A 4 ? 0.7382 0.6770 0.7460 -0.0050 -0.0496 -0.0118 3 ILE A CA 24 C C . ILE A 4 ? 0.6751 0.6183 0.6883 -0.0057 -0.0455 -0.0149 3 ILE A C 25 O O . ILE A 4 ? 0.6074 0.5472 0.6191 -0.0032 -0.0434 -0.0153 3 ILE A O 26 C CB . ILE A 4 ? 0.7815 0.7152 0.7862 -0.0031 -0.0522 -0.0090 3 ILE A CB 27 C CG1 . ILE A 4 ? 0.8715 0.8009 0.8704 -0.0022 -0.0560 -0.0060 3 ILE A CG1 28 C CG2 . ILE A 4 ? 0.6905 0.6281 0.7004 -0.0052 -0.0527 -0.0090 3 ILE A CG2 29 C CD1 . ILE A 4 ? 0.9201 0.8535 0.9212 -0.0053 -0.0583 -0.0053 3 ILE A CD1 30 N N . VAL A 5 ? 0.6115 0.5635 0.6311 -0.0092 -0.0441 -0.0168 4 VAL A N 31 C CA . VAL A 5 ? 0.5841 0.5412 0.6093 -0.0103 -0.0400 -0.0198 4 VAL A CA 32 C C . VAL A 5 ? 0.6726 0.6380 0.7039 -0.0136 -0.0396 -0.0198 4 VAL A C 33 O O . VAL A 5 ? 0.7247 0.6919 0.7558 -0.0150 -0.0422 -0.0176 4 VAL A O 34 C CB . VAL A 5 ? 0.5763 0.5385 0.6029 -0.0105 -0.0360 -0.0224 4 VAL A CB 35 C CG1 . VAL A 5 ? 0.5588 0.5131 0.5791 -0.0067 -0.0354 -0.0222 4 VAL A CG1 36 C CG2 . VAL A 5 ? 0.5975 0.5685 0.6256 -0.0130 -0.0356 -0.0218 4 VAL A CG2 37 N N . GLU A 6 ? 0.6820 0.6524 0.7184 -0.0148 -0.0358 -0.0222 5 GLU A N 38 C CA . GLU A 6 ? 0.6455 0.6242 0.6873 -0.0179 -0.0345 -0.0223 5 GLU A CA 39 C C . GLU A 6 ? 0.6163 0.6049 0.6617 -0.0205 -0.0313 -0.0241 5 GLU A C 40 O O . GLU A 6 ? 0.5865 0.5760 0.6324 -0.0199 -0.0287 -0.0265 5 GLU A O 41 C CB . GLU A 6 ? 0.5422 0.5204 0.5869 -0.0175 -0.0322 -0.0234 5 GLU A CB 42 C CG . GLU A 6 ? 0.7363 0.7170 0.7835 -0.0191 -0.0328 -0.0219 5 GLU A CG 43 C CD . GLU A 6 ? 0.8711 0.8614 0.9217 -0.0224 -0.0310 -0.0219 5 GLU A CD 44 O OE1 . GLU A 6 ? 0.9424 0.9393 0.9955 -0.0240 -0.0276 -0.0237 5 GLU A OE1 45 O OE2 . GLU A 6 ? 0.9373 0.9289 0.9879 -0.0235 -0.0328 -0.0200 5 GLU A OE2 46 N N . PRO A 7 ? 0.7493 0.7452 0.7964 -0.0232 -0.0312 -0.0230 6 PRO A N 47 C CA . PRO A 7 ? 0.6992 0.7042 0.7486 -0.0254 -0.0281 -0.0243 6 PRO A CA 48 C C . PRO A 7 ? 0.6002 0.6102 0.6533 -0.0262 -0.0232 -0.0266 6 PRO A C 49 O O . PRO A 7 ? 0.6500 0.6644 0.7041 -0.0265 -0.0203 -0.0283 6 PRO A O 50 C CB . PRO A 7 ? 0.7845 0.7949 0.8340 -0.0277 -0.0289 -0.0221 6 PRO A CB 51 C CG . PRO A 7 ? 0.7662 0.7715 0.8154 -0.0270 -0.0311 -0.0206 6 PRO A CG 52 C CD . PRO A 7 ? 0.8141 0.8099 0.8599 -0.0239 -0.0341 -0.0202 6 PRO A CD 53 N N . HIS A 8 ? 0.6181 0.6273 0.6731 -0.0263 -0.0222 -0.0266 7 HIS A N 54 C CA . HIS A 8 ? 0.6497 0.6640 0.7080 -0.0270 -0.0177 -0.0282 7 HIS A CA 55 C C . HIS A 8 ? 0.5023 0.5118 0.5619 -0.0255 -0.0172 -0.0290 7 HIS A C 56 O O . HIS A 8 ? 0.5808 0.5864 0.6397 -0.0253 -0.0198 -0.0273 7 HIS A O 57 C CB . HIS A 8 ? 0.6802 0.7017 0.7398 -0.0295 -0.0166 -0.0265 7 HIS A CB 58 C CG . HIS A 8 ? 0.7279 0.7550 0.7866 -0.0309 -0.0162 -0.0257 7 HIS A CG 59 N ND1 . HIS A 8 ? 0.8164 0.8429 0.8725 -0.0315 -0.0195 -0.0240 7 HIS A ND1 60 C CD2 . HIS A 8 ? 0.7377 0.7707 0.7976 -0.0313 -0.0128 -0.0264 7 HIS A CD2 61 C CE1 . HIS A 8 ? 0.8262 0.8582 0.8823 -0.0325 -0.0183 -0.0234 7 HIS A CE1 62 N NE2 . HIS A 8 ? 0.8445 0.8804 0.9029 -0.0322 -0.0142 -0.0249 7 HIS A NE2 63 N N . VAL A 9 ? 0.5095 0.5195 0.5710 -0.0244 -0.0136 -0.0314 8 VAL A N 64 C CA . VAL A 9 ? 0.4352 0.4407 0.4979 -0.0228 -0.0130 -0.0320 8 VAL A CA 65 C C . VAL A 9 ? 0.4621 0.4735 0.5284 -0.0234 -0.0083 -0.0335 8 VAL A C 66 O O . VAL A 9 ? 0.4825 0.4993 0.5498 -0.0238 -0.0050 -0.0351 8 VAL A O 67 C CB . VAL A 9 ? 0.4900 0.4878 0.5502 -0.0198 -0.0137 -0.0331 8 VAL A CB 68 C CG1 . VAL A 9 ? 0.4545 0.4498 0.5163 -0.0181 -0.0114 -0.0342 8 VAL A CG1 69 C CG2 . VAL A 9 ? 0.5822 0.5721 0.6379 -0.0185 -0.0189 -0.0308 8 VAL A CG2 70 N N . THR A 10 ? 0.4719 0.4825 0.5398 -0.0235 -0.0081 -0.0329 9 THR A N 71 C CA . THR A 10 ? 0.3883 0.4032 0.4593 -0.0235 -0.0039 -0.0343 9 THR A CA 72 C C . THR A 10 ? 0.3870 0.3976 0.4592 -0.0212 -0.0023 -0.0360 9 THR A C 73 O O . THR A 10 ? 0.3937 0.3979 0.4647 -0.0198 -0.0050 -0.0351 9 THR A O 74 C CB . THR A 10 ? 0.2979 0.3150 0.3699 -0.0251 -0.0044 -0.0324 9 THR A CB 75 O OG1 . THR A 10 ? 0.4730 0.4939 0.5434 -0.0272 -0.0058 -0.0306 9 THR A OG1 76 C CG2 . THR A 10 ? 0.3866 0.4073 0.4610 -0.0249 -0.0002 -0.0339 9 THR A CG2 77 N N . ALA A 11 ? 0.3839 0.3980 0.4581 -0.0205 0.0022 -0.0385 10 ALA A N 78 C CA . ALA A 11 ? 0.2586 0.2696 0.3339 -0.0182 0.0044 -0.0403 10 ALA A CA 79 C C . ALA A 11 ? 0.3384 0.3540 0.4169 -0.0182 0.0088 -0.0419 10 ALA A C 80 O O . ALA A 11 ? 0.3739 0.3948 0.4524 -0.0194 0.0113 -0.0427 10 ALA A O 81 C CB . ALA A 11 ? 0.3272 0.3377 0.4011 -0.0169 0.0057 -0.0421 10 ALA A CB 82 N N . VAL A 12 ? 0.3088 0.3218 0.3891 -0.0167 0.0097 -0.0423 11 VAL A N 83 C CA . VAL A 12 ? 0.2793 0.2958 0.3623 -0.0166 0.0137 -0.0437 11 VAL A CA 84 C C . VAL A 12 ? 0.3264 0.3437 0.4111 -0.0146 0.0178 -0.0464 11 VAL A C 85 O O . VAL A 12 ? 0.3002 0.3142 0.3849 -0.0131 0.0168 -0.0458 11 VAL A O 86 C CB . VAL A 12 ? 0.3722 0.3863 0.4566 -0.0166 0.0120 -0.0420 11 VAL A CB 87 C CG1 . VAL A 12 ? 0.3078 0.3247 0.3944 -0.0163 0.0161 -0.0437 11 VAL A CG1 88 C CG2 . VAL A 12 ? 0.2110 0.2250 0.2938 -0.0187 0.0082 -0.0393 11 VAL A CG2 89 N N . TRP A 13 ? 0.2927 0.3135 0.3773 -0.0148 0.0220 -0.0489 12 TRP A N 90 C CA . TRP A 13 ? 0.2998 0.3208 0.3835 -0.0136 0.0251 -0.0503 12 TRP A CA 91 C C . TRP A 13 ? 0.3211 0.3404 0.4065 -0.0125 0.0249 -0.0484 12 TRP A C 92 O O . TRP A 13 ? 0.3322 0.3508 0.4195 -0.0123 0.0250 -0.0483 12 TRP A O 93 C CB . TRP A 13 ? 0.2361 0.2573 0.3146 -0.0150 0.0266 -0.0510 12 TRP A CB 94 C CG . TRP A 13 ? 0.3680 0.3874 0.4415 -0.0151 0.0271 -0.0501 12 TRP A CG 95 C CD1 . TRP A 13 ? 0.3364 0.3564 0.4066 -0.0160 0.0270 -0.0506 12 TRP A CD1 96 C CD2 . TRP A 13 ? 0.2611 0.2773 0.3326 -0.0147 0.0270 -0.0487 12 TRP A CD2 97 N NE1 . TRP A 13 ? 0.2862 0.3038 0.3533 -0.0168 0.0267 -0.0494 12 TRP A NE1 98 C CE2 . TRP A 13 ? 0.2545 0.2699 0.3227 -0.0165 0.0265 -0.0482 12 TRP A CE2 99 C CE3 . TRP A 13 ? 0.2773 0.2919 0.3503 -0.0137 0.0271 -0.0477 12 TRP A CE3 100 C CZ2 . TRP A 13 ? 0.3269 0.3416 0.3947 -0.0174 0.0264 -0.0465 12 TRP A CZ2 101 C CZ3 . TRP A 13 ? 0.3506 0.3631 0.4224 -0.0162 0.0260 -0.0458 12 TRP A CZ3 102 C CH2 . TRP A 13 ? 0.2746 0.2883 0.3444 -0.0172 0.0264 -0.0453 12 TRP A CH2 103 N N . GLY A 14 ? 0.3897 0.4088 0.4752 -0.0122 0.0245 -0.0471 13 GLY A N 104 C CA . GLY A 14 ? 0.3236 0.3410 0.4106 -0.0119 0.0242 -0.0457 13 GLY A CA 105 C C . GLY A 14 ? 0.3942 0.4071 0.4823 -0.0102 0.0211 -0.0447 13 GLY A C 106 O O . GLY A 14 ? 0.3410 0.3500 0.4264 -0.0092 0.0201 -0.0430 13 GLY A O 107 N N . LYS A 15 ? 0.3772 0.3865 0.4625 -0.0100 0.0178 -0.0442 14 LYS A N 108 C CA . LYS A 15 ? 0.3619 0.3630 0.4421 -0.0088 0.0128 -0.0416 14 LYS A CA 109 C C . LYS A 15 ? 0.3602 0.3551 0.4335 -0.0075 0.0094 -0.0402 14 LYS A C 110 O O . LYS A 15 ? 0.3255 0.3209 0.3967 -0.0069 0.0107 -0.0407 14 LYS A O 111 C CB . LYS A 15 ? 0.3488 0.3504 0.4312 -0.0102 0.0110 -0.0412 14 LYS A CB 112 C CG . LYS A 15 ? 0.3269 0.3332 0.4146 -0.0108 0.0142 -0.0422 14 LYS A CG 113 C CD . LYS A 15 ? 0.3250 0.3286 0.4126 -0.0114 0.0111 -0.0403 14 LYS A CD 114 C CE . LYS A 15 ? 0.4906 0.4983 0.5824 -0.0119 0.0143 -0.0414 14 LYS A CE 115 N NZ . LYS A 15 ? 0.4489 0.4569 0.5433 -0.0105 0.0165 -0.0417 14 LYS A NZ 116 N N . ASN A 16 ? 0.4333 0.4223 0.5029 -0.0072 0.0050 -0.0383 15 ASN A N 117 C CA . ASN A 16 ? 0.3541 0.3360 0.4163 -0.0056 0.0015 -0.0365 15 ASN A CA 118 C C . ASN A 16 ? 0.4177 0.3996 0.4801 -0.0073 -0.0013 -0.0363 15 ASN A C 119 O O . ASN A 16 ? 0.3049 0.2905 0.3716 -0.0095 -0.0017 -0.0364 15 ASN A O 120 C CB . ASN A 16 ? 0.2758 0.2498 0.3320 -0.0036 -0.0013 -0.0339 15 ASN A CB 121 C CG . ASN A 16 ? 0.4603 0.4340 0.5155 -0.0021 0.0009 -0.0336 15 ASN A CG 122 O OD1 . ASN A 16 ? 0.5463 0.5238 0.6029 -0.0019 0.0041 -0.0349 15 ASN A OD1 123 N ND2 . ASN A 16 ? 0.5513 0.5204 0.6036 -0.0012 -0.0007 -0.0318 15 ASN A ND2 124 N N . VAL A 17 ? 0.3519 0.3297 0.4091 -0.0064 -0.0034 -0.0356 16 VAL A N 125 C CA . VAL A 17 ? 0.4022 0.3784 0.4580 -0.0076 -0.0070 -0.0345 16 VAL A CA 126 C C . VAL A 17 ? 0.4416 0.4098 0.4896 -0.0052 -0.0098 -0.0326 16 VAL A C 127 O O . VAL A 17 ? 0.4164 0.3817 0.4601 -0.0029 -0.0082 -0.0324 16 VAL A O 128 C CB . VAL A 17 ? 0.4827 0.4657 0.5421 -0.0101 -0.0059 -0.0363 16 VAL A CB 129 C CG1 . VAL A 17 ? 0.4328 0.4236 0.4985 -0.0127 -0.0033 -0.0375 16 VAL A CG1 130 C CG2 . VAL A 17 ? 0.2667 0.2505 0.3243 -0.0089 -0.0033 -0.0379 16 VAL A CG2 131 N N . SER A 18 ? 0.4635 0.4288 0.5095 -0.0057 -0.0137 -0.0308 17 SER A N 132 C CA . SER A 18 ? 0.4530 0.4118 0.4921 -0.0038 -0.0164 -0.0289 17 SER A CA 133 C C . SER A 18 ? 0.4327 0.3942 0.4727 -0.0052 -0.0175 -0.0297 17 SER A C 134 O O . SER A 18 ? 0.4192 0.3855 0.4635 -0.0081 -0.0186 -0.0301 17 SER A O 135 C CB . SER A 18 ? 0.4748 0.4287 0.5110 -0.0031 -0.0201 -0.0261 17 SER A CB 136 O OG . SER A 18 ? 0.6018 0.5523 0.6352 -0.0012 -0.0190 -0.0251 17 SER A OG 137 N N . LEU A 19 ? 0.4042 0.3630 0.4399 -0.0035 -0.0170 -0.0298 18 LEU A N 138 C CA . LEU A 19 ? 0.4274 0.3873 0.4626 -0.0045 -0.0188 -0.0300 18 LEU A CA 139 C C . LEU A 19 ? 0.4694 0.4219 0.4979 -0.0024 -0.0226 -0.0269 18 LEU A C 140 O O . LEU A 19 ? 0.4299 0.3776 0.4529 0.0004 -0.0218 -0.0257 18 LEU A O 141 C CB . LEU A 19 ? 0.4039 0.3668 0.4392 -0.0041 -0.0154 -0.0324 18 LEU A CB 142 C CG . LEU A 19 ? 0.4236 0.3956 0.4661 -0.0065 -0.0113 -0.0355 18 LEU A CG 143 C CD1 . LEU A 19 ? 0.4021 0.3783 0.4451 -0.0068 -0.0086 -0.0377 18 LEU A CD1 144 C CD2 . LEU A 19 ? 0.4845 0.4625 0.5325 -0.0101 -0.0126 -0.0355 18 LEU A CD2 145 N N . LYS A 20 ? 0.5287 0.4810 0.5578 -0.0039 -0.0265 -0.0253 19 LYS A N 146 C CA . LYS A 20 ? 0.5679 0.5140 0.5912 -0.0020 -0.0303 -0.0220 19 LYS A CA 147 C C . LYS A 20 ? 0.5286 0.4728 0.5481 -0.0015 -0.0321 -0.0213 19 LYS A C 148 O O . LYS A 20 ? 0.4937 0.4424 0.5161 -0.0038 -0.0322 -0.0228 19 LYS A O 149 C CB . LYS A 20 ? 0.5853 0.5321 0.6108 -0.0038 -0.0336 -0.0204 19 LYS A CB 150 C CG . LYS A 20 ? 0.6722 0.6150 0.6932 -0.0031 -0.0382 -0.0174 19 LYS A CG 151 C CD . LYS A 20 ? 0.7727 0.7194 0.7975 -0.0060 -0.0407 -0.0167 19 LYS A CD 152 C CE . LYS A 20 ? 0.7993 0.7417 0.8199 -0.0052 -0.0453 -0.0134 19 LYS A CE 153 N NZ . LYS A 20 ? 0.6482 0.5949 0.6726 -0.0080 -0.0473 -0.0125 19 LYS A NZ 154 N N . CYS A 21 ? 0.4830 0.4216 0.4960 0.0013 -0.0332 -0.0190 20 CYS A N 155 C CA . CYS A 21 ? 0.5156 0.4519 0.5244 0.0020 -0.0351 -0.0179 20 CYS A CA 156 C C . CYS A 21 ? 0.5466 0.4777 0.5490 0.0044 -0.0371 -0.0148 20 CYS A C 157 O O . CYS A 21 ? 0.6120 0.5413 0.6117 0.0063 -0.0348 -0.0144 20 CYS A O 158 C CB . CYS A 21 ? 0.5153 0.4529 0.5237 0.0028 -0.0316 -0.0200 20 CYS A CB 159 S SG . CYS A 21 ? 0.6473 0.5822 0.6508 0.0035 -0.0338 -0.0186 20 CYS A SG 160 N N . LEU A 22 ? 0.5664 0.4957 0.5667 0.0038 -0.0413 -0.0126 21 LEU A N 161 C CA . LEU A 22 ? 0.6741 0.5995 0.6685 0.0055 -0.0434 -0.0099 21 LEU A CA 162 C C . LEU A 22 ? 0.6857 0.6094 0.6759 0.0059 -0.0449 -0.0088 21 LEU A C 163 O O . LEU A 22 ? 0.6588 0.5836 0.6508 0.0042 -0.0469 -0.0089 21 LEU A O 164 C CB . LEU A 22 ? 0.6853 0.6103 0.6802 0.0045 -0.0470 -0.0082 21 LEU A CB 165 C CG . LEU A 22 ? 0.5702 0.4964 0.5683 0.0043 -0.0457 -0.0089 21 LEU A CG 166 C CD1 . LEU A 22 ? 0.7320 0.6578 0.7306 0.0033 -0.0495 -0.0072 21 LEU A CD1 167 C CD2 . LEU A 22 ? 0.6260 0.5507 0.6213 0.0063 -0.0426 -0.0092 21 LEU A CD2 168 N N . ILE A 23 ? 0.6356 0.5569 0.6207 0.0079 -0.0438 -0.0078 22 ILE A N 169 C CA . ILE A 23 ? 0.8332 0.7531 0.8142 0.0085 -0.0444 -0.0070 22 ILE A CA 170 C C . ILE A 23 ? 0.9424 0.8598 0.9181 0.0091 -0.0462 -0.0050 22 ILE A C 171 O O . ILE A 23 ? 0.9127 0.8294 0.8864 0.0103 -0.0444 -0.0049 22 ILE A O 172 C CB . ILE A 23 ? 0.7937 0.7139 0.7739 0.0100 -0.0403 -0.0082 22 ILE A CB 173 C CG1 . ILE A 23 ? 0.5855 0.5086 0.5710 0.0093 -0.0376 -0.0109 22 ILE A CG1 174 C CG2 . ILE A 23 ? 0.7441 0.6629 0.7204 0.0105 -0.0411 -0.0073 22 ILE A CG2 175 C CD1 . ILE A 23 ? 0.5483 0.4720 0.5331 0.0109 -0.0333 -0.0121 22 ILE A CD1 176 N N . GLU A 24 ? 0.9025 0.8190 0.8763 0.0081 -0.0496 -0.0036 23 GLU A N 177 C CA . GLU A 24 ? 1.0356 0.9502 1.0044 0.0085 -0.0506 -0.0024 23 GLU A CA 178 C C . GLU A 24 ? 1.0743 0.9884 1.0411 0.0079 -0.0520 -0.0015 23 GLU A C 179 O O . GLU A 24 ? 1.0576 0.9716 1.0245 0.0063 -0.0552 -0.0005 23 GLU A O 180 C CB . GLU A 24 ? 1.1001 1.0140 1.0686 0.0075 -0.0531 -0.0017 23 GLU A CB 181 C CG . GLU A 24 ? 1.2332 1.1451 1.1968 0.0076 -0.0539 -0.0009 23 GLU A CG 182 C CD . GLU A 24 ? 1.2156 1.1265 1.1769 0.0089 -0.0518 -0.0011 23 GLU A CD 183 O OE1 . GLU A 24 ? 1.4445 1.3560 1.4076 0.0096 -0.0501 -0.0018 23 GLU A OE1 184 O OE2 . GLU A 24 ? 1.1958 1.1041 1.1527 0.0090 -0.0530 -0.0009 23 GLU A OE2 185 N N . VAL A 25 ? 1.0740 0.9878 1.0392 0.0091 -0.0496 -0.0018 24 VAL A N 186 C CA . VAL A 25 ? 1.1507 1.0644 1.1145 0.0086 -0.0507 -0.0009 24 VAL A CA 187 C C . VAL A 25 ? 1.1804 1.0926 1.1398 0.0086 -0.0512 0.0003 24 VAL A C 188 O O . VAL A 25 ? 1.1735 1.0858 1.1319 0.0078 -0.0523 0.0013 24 VAL A O 189 C CB . VAL A 25 ? 1.0480 0.9621 1.0119 0.0098 -0.0480 -0.0017 24 VAL A CB 190 C CG1 . VAL A 25 ? 0.9995 0.9137 0.9623 0.0092 -0.0493 -0.0006 24 VAL A CG1 191 C CG2 . VAL A 25 ? 0.9577 0.8735 0.9267 0.0095 -0.0468 -0.0036 24 VAL A CG2 192 N N . ASN A 26 ? 1.0185 0.9296 0.9757 0.0090 -0.0507 0.0002 25 ASN A N 193 C CA . ASN A 26 ? 0.9702 0.8798 0.9236 0.0093 -0.0502 0.0009 25 ASN A CA 194 C C . ASN A 26 ? 1.0211 0.9304 0.9721 0.0110 -0.0470 0.0007 25 ASN A C 195 O O . ASN A 26 ? 0.9733 0.8803 0.9205 0.0112 -0.0474 0.0009 25 ASN A O 196 C CB . ASN A 26 ? 1.0983 1.0078 1.0507 0.0080 -0.0520 0.0020 25 ASN A CB 197 C CG . ASN A 26 ? 1.2722 1.1825 1.2242 0.0085 -0.0508 0.0025 25 ASN A CG 198 O OD1 . ASN A 26 ? 1.1885 1.0986 1.1386 0.0099 -0.0482 0.0024 25 ASN A OD1 199 N ND2 . ASN A 26 ? 1.2700 1.1816 1.2242 0.0071 -0.0527 0.0032 25 ASN A ND2 200 N N . GLU A 27 ? 1.0134 0.9234 0.9650 0.0122 -0.0446 0.0002 26 GLU A N 201 C CA . GLU A 27 ? 0.8130 0.7226 0.7622 0.0135 -0.0420 0.0002 26 GLU A CA 202 C C . GLU A 27 ? 0.6527 0.5624 0.6026 0.0148 -0.0398 -0.0009 26 GLU A C 203 O O . GLU A 27 ? 0.6980 0.6094 0.6516 0.0146 -0.0391 -0.0015 26 GLU A O 204 C CB . GLU A 27 ? 0.7603 0.6705 0.7088 0.0136 -0.0415 0.0009 26 GLU A CB 205 C CG . GLU A 27 ? 0.7844 0.6956 0.7350 0.0137 -0.0412 0.0004 26 GLU A CG 206 C CD . GLU A 27 ? 0.8597 0.7712 0.8091 0.0137 -0.0412 0.0013 26 GLU A CD 207 O OE1 . GLU A 27 ? 0.6974 0.6093 0.6465 0.0149 -0.0389 0.0009 26 GLU A OE1 208 O OE2 . GLU A 27 ? 0.8938 0.8053 0.8427 0.0125 -0.0434 0.0025 26 GLU A OE2 209 N N . THR A 28 ? 0.6342 0.5421 0.5804 0.0161 -0.0386 -0.0012 27 THR A N 210 C CA . THR A 28 ? 0.5993 0.5068 0.5454 0.0173 -0.0367 -0.0022 27 THR A CA 211 C C . THR A 28 ? 0.6496 0.5608 0.6011 0.0174 -0.0338 -0.0027 27 THR A C 212 O O . THR A 28 ? 0.4861 0.3995 0.4396 0.0173 -0.0322 -0.0024 27 THR A O 213 C CB . THR A 28 ? 0.5982 0.5033 0.5394 0.0186 -0.0360 -0.0022 27 THR A CB 214 O OG1 . THR A 28 ? 0.8251 0.7269 0.7617 0.0182 -0.0385 -0.0018 27 THR A OG1 215 C CG2 . THR A 28 ? 0.6825 0.5862 0.6222 0.0197 -0.0351 -0.0031 27 THR A CG2 216 N N . ILE A 29 ? 0.6720 0.5840 0.6263 0.0176 -0.0331 -0.0036 28 ILE A N 217 C CA . ILE A 29 ? 0.5389 0.4543 0.4988 0.0174 -0.0302 -0.0046 28 ILE A CA 218 C C . ILE A 29 ? 0.4599 0.3753 0.4192 0.0187 -0.0276 -0.0055 28 ILE A C 219 O O . ILE A 29 ? 0.4849 0.3983 0.4418 0.0196 -0.0280 -0.0058 28 ILE A O 220 C CB . ILE A 29 ? 0.5630 0.4794 0.5266 0.0166 -0.0308 -0.0053 28 ILE A CB 221 C CG1 . ILE A 29 ? 0.6139 0.5294 0.5773 0.0153 -0.0345 -0.0047 28 ILE A CG1 222 C CG2 . ILE A 29 ? 0.5521 0.4708 0.5202 0.0166 -0.0279 -0.0070 28 ILE A CG2 223 C CD1 . ILE A 29 ? 0.6227 0.5389 0.5897 0.0144 -0.0356 -0.0054 28 ILE A CD1 224 N N . THR A 30 ? 0.4591 0.3768 0.4207 0.0189 -0.0249 -0.0059 29 THR A N 225 C CA . THR A 30 ? 0.4237 0.3418 0.3849 0.0201 -0.0223 -0.0068 29 THR A CA 226 C C . THR A 30 ? 0.5097 0.4305 0.4762 0.0198 -0.0196 -0.0085 29 THR A C 227 O O . THR A 30 ? 0.6126 0.5330 0.5784 0.0208 -0.0183 -0.0091 29 THR A O 228 C CB . THR A 30 ? 0.5142 0.4334 0.4747 0.0204 -0.0209 -0.0064 29 THR A CB 229 O OG1 . THR A 30 ? 0.4950 0.4167 0.4586 0.0208 -0.0175 -0.0078 29 THR A OG1 230 C CG2 . THR A 30 ? 0.5114 0.4304 0.4718 0.0197 -0.0227 -0.0061 29 THR A CG2 231 N N . GLN A 31 ? 0.3759 0.2990 0.3470 0.0186 -0.0189 -0.0096 30 GLN A N 232 C CA . GLN A 31 ? 0.4126 0.3381 0.3886 0.0180 -0.0165 -0.0115 30 GLN A CA 233 C C . GLN A 31 ? 0.4319 0.3575 0.4096 0.0170 -0.0184 -0.0129 30 GLN A C 234 O O . GLN A 31 ? 0.3859 0.3103 0.3619 0.0167 -0.0210 -0.0127 30 GLN A O 235 C CB . GLN A 31 ? 0.4306 0.3588 0.4091 0.0184 -0.0125 -0.0131 30 GLN A CB 236 C CG . GLN A 31 ? 0.4098 0.3396 0.3896 0.0181 -0.0116 -0.0151 30 GLN A CG 237 C CD . GLN A 31 ? 0.4304 0.3631 0.4121 0.0185 -0.0077 -0.0163 30 GLN A CD 238 O OE1 . GLN A 31 ? 0.4119 0.3441 0.3923 0.0193 -0.0070 -0.0151 30 GLN A OE1 239 N NE2 . GLN A 31 ? 0.3327 0.2680 0.3167 0.0179 -0.0057 -0.0189 30 GLN A NE2 240 N N . ILE A 32 ? 0.3957 0.3229 0.3773 0.0162 -0.0171 -0.0143 31 ILE A N 241 C CA . ILE A 32 ? 0.3906 0.3186 0.3750 0.0148 -0.0189 -0.0159 31 ILE A CA 242 C C . ILE A 32 ? 0.4621 0.3936 0.4510 0.0141 -0.0150 -0.0188 31 ILE A C 243 O O . ILE A 32 ? 0.4937 0.4264 0.4835 0.0146 -0.0113 -0.0189 31 ILE A O 244 C CB . ILE A 32 ? 0.3842 0.3107 0.3686 0.0142 -0.0217 -0.0146 31 ILE A CB 245 C CG1 . ILE A 32 ? 0.4231 0.3507 0.4097 0.0144 -0.0187 -0.0149 31 ILE A CG1 246 C CG2 . ILE A 32 ? 0.5400 0.4636 0.5197 0.0149 -0.0247 -0.0119 31 ILE A CG2 247 C CD1 . ILE A 32 ? 0.5023 0.4285 0.4886 0.0140 -0.0210 -0.0137 31 ILE A CD1 248 N N . SER A 33 ? 0.4564 0.3903 0.4486 0.0126 -0.0158 -0.0212 32 SER A N 249 C CA . SER A 33 ? 0.3133 0.2515 0.3095 0.0117 -0.0119 -0.0242 32 SER A CA 250 C C . SER A 33 ? 0.3744 0.3166 0.3760 0.0093 -0.0135 -0.0269 32 SER A C 251 O O . SER A 33 ? 0.4200 0.3618 0.4222 0.0081 -0.0175 -0.0267 32 SER A O 252 C CB . SER A 33 ? 0.3294 0.2693 0.3245 0.0124 -0.0092 -0.0254 32 SER A CB 253 O OG . SER A 33 ? 0.4251 0.3683 0.4227 0.0111 -0.0108 -0.0279 32 SER A OG 254 N N . TRP A 34 ? 0.3692 0.3157 0.3750 0.0082 -0.0104 -0.0292 33 TRP A N 255 C CA . TRP A 34 ? 0.3035 0.2570 0.3167 0.0053 -0.0103 -0.0325 33 TRP A CA 256 C C . TRP A 34 ? 0.3355 0.2957 0.3517 0.0047 -0.0061 -0.0354 33 TRP A C 257 O O . TRP A 34 ? 0.3502 0.3096 0.3635 0.0065 -0.0030 -0.0348 33 TRP A O 258 C CB . TRP A 34 ? 0.2525 0.2074 0.2691 0.0043 -0.0095 -0.0327 33 TRP A CB 259 C CG . TRP A 34 ? 0.4332 0.3853 0.4504 0.0034 -0.0137 -0.0309 33 TRP A CG 260 C CD1 . TRP A 34 ? 0.3734 0.3198 0.3866 0.0049 -0.0151 -0.0280 33 TRP A CD1 261 C CD2 . TRP A 34 ? 0.3426 0.2986 0.3649 0.0002 -0.0165 -0.0319 33 TRP A CD2 262 N NE1 . TRP A 34 ? 0.3945 0.3405 0.4096 0.0034 -0.0188 -0.0270 33 TRP A NE1 263 C CE2 . TRP A 34 ? 0.3192 0.2706 0.3396 0.0005 -0.0198 -0.0291 33 TRP A CE2 264 C CE3 . TRP A 34 ? 0.3705 0.3350 0.3982 -0.0032 -0.0159 -0.0340 33 TRP A CE3 265 C CZ2 . TRP A 34 ? 0.3339 0.2878 0.3579 -0.0022 -0.0231 -0.0287 33 TRP A CZ2 266 C CZ3 . TRP A 34 ? 0.3507 0.3190 0.3811 -0.0060 -0.0186 -0.0326 33 TRP A CZ3 267 C CH2 . TRP A 34 ? 0.4173 0.3791 0.4465 -0.0056 -0.0227 -0.0307 33 TRP A CH2 268 N N . GLU A 35 ? 0.3061 0.2743 0.3272 0.0016 -0.0058 -0.0375 34 GLU A N 269 C CA . GLU A 35 ? 0.3673 0.3437 0.3909 0.0005 -0.0014 -0.0396 34 GLU A CA 270 C C . GLU A 35 ? 0.3425 0.3300 0.3734 -0.0037 0.0005 -0.0413 34 GLU A C 271 O O . GLU A 35 ? 0.4034 0.3930 0.4365 -0.0060 -0.0021 -0.0401 34 GLU A O 272 C CB . GLU A 35 ? 0.4258 0.4029 0.4451 0.0011 -0.0021 -0.0377 34 GLU A CB 273 C CG . GLU A 35 ? 0.4676 0.4336 0.4796 0.0053 -0.0037 -0.0361 34 GLU A CG 274 C CD . GLU A 35 ? 0.7072 0.6739 0.7151 0.0061 -0.0036 -0.0345 34 GLU A CD 275 O OE1 . GLU A 35 ? 0.7081 0.6841 0.7187 0.0033 -0.0025 -0.0346 34 GLU A OE1 276 O OE2 . GLU A 35 ? 0.7460 0.7040 0.7480 0.0095 -0.0047 -0.0332 34 GLU A OE2 277 N N . LYS A 36 ? 0.3790 0.3733 0.4135 -0.0046 0.0052 -0.0441 35 LYS A N 278 C CA . LYS A 36 ? 0.4617 0.4667 0.5031 -0.0086 0.0078 -0.0460 35 LYS A CA 279 C C . LYS A 36 ? 0.5392 0.5529 0.5813 -0.0106 0.0098 -0.0462 35 LYS A C 280 O O . LYS A 36 ? 0.6293 0.6428 0.6691 -0.0089 0.0122 -0.0470 35 LYS A O 281 C CB . LYS A 36 ? 0.4943 0.5010 0.5398 -0.0084 0.0119 -0.0489 35 LYS A CB 282 C CG . LYS A 36 ? 0.4880 0.5050 0.5408 -0.0125 0.0146 -0.0513 35 LYS A CG 283 C CD . LYS A 36 ? 0.4086 0.4253 0.4643 -0.0144 0.0118 -0.0504 35 LYS A CD 284 C CE . LYS A 36 ? 0.4577 0.4846 0.5197 -0.0175 0.0151 -0.0515 35 LYS A CE 285 N NZ . LYS A 36 ? 0.4201 0.4491 0.4847 -0.0163 0.0198 -0.0534 35 LYS A NZ 286 N N . ILE A 37 ? 0.5542 0.5756 0.5997 -0.0142 0.0088 -0.0456 36 ILE A N 287 C CA . ILE A 37 ? 0.5702 0.6002 0.6165 -0.0164 0.0103 -0.0455 36 ILE A CA 288 C C . ILE A 37 ? 0.6242 0.6624 0.6753 -0.0181 0.0156 -0.0489 36 ILE A C 289 O O . ILE A 37 ? 0.6453 0.6879 0.7018 -0.0203 0.0175 -0.0509 36 ILE A O 290 C CB . ILE A 37 ? 0.5481 0.5837 0.5966 -0.0197 0.0075 -0.0437 36 ILE A CB 291 C CG1 . ILE A 37 ? 0.4568 0.4850 0.4996 -0.0179 0.0025 -0.0401 36 ILE A CG1 292 C CG2 . ILE A 37 ? 0.5412 0.5877 0.5925 -0.0227 0.0102 -0.0446 36 ILE A CG2 293 C CD1 . ILE A 37 ? 0.4705 0.5035 0.5150 -0.0209 -0.0004 -0.0383 36 ILE A CD1 294 N N . HIS A 38 ? 0.7788 0.8191 0.8280 -0.0172 0.0182 -0.0496 37 HIS A N 295 C CA . HIS A 38 ? 0.7314 0.7779 0.7831 -0.0185 0.0226 -0.0520 37 HIS A CA 296 C C . HIS A 38 ? 0.8971 0.9477 0.9454 -0.0196 0.0224 -0.0504 37 HIS A C 297 O O . HIS A 38 ? 0.9768 1.0260 1.0225 -0.0178 0.0230 -0.0498 37 HIS A O 298 C CB . HIS A 38 ? 0.7348 0.7743 0.7840 -0.0158 0.0234 -0.0515 37 HIS A CB 299 C CG . HIS A 38 ? 0.8741 0.9101 0.9258 -0.0155 0.0233 -0.0518 37 HIS A CG 300 N ND1 . HIS A 38 ? 0.8732 0.9012 0.9221 -0.0120 0.0227 -0.0500 37 HIS A ND1 301 C CD2 . HIS A 38 ? 0.8912 0.9295 0.9465 -0.0181 0.0234 -0.0535 37 HIS A CD2 302 C CE1 . HIS A 38 ? 0.8293 0.8567 0.8815 -0.0127 0.0227 -0.0503 37 HIS A CE1 303 N NE2 . HIS A 38 ? 0.8733 0.9072 0.9303 -0.0166 0.0234 -0.0527 37 HIS A NE2 304 N N . GLY A 39 ? 0.9228 0.9771 0.9699 -0.0217 0.0217 -0.0491 38 GLY A N 305 C CA . GLY A 39 ? 0.9358 0.9941 0.9802 -0.0226 0.0211 -0.0472 38 GLY A CA 306 C C . GLY A 39 ? 0.9045 0.9653 0.9505 -0.0232 0.0189 -0.0457 38 GLY A C 307 O O . GLY A 39 ? 0.8295 0.8898 0.8779 -0.0241 0.0164 -0.0449 38 GLY A O 308 N N . LYS A 40 ? 1.0063 1.0689 1.0507 -0.0227 0.0191 -0.0450 39 LYS A N 309 C CA . LYS A 40 ? 1.0664 1.1266 1.1090 -0.0221 0.0154 -0.0426 39 LYS A CA 310 C C . LYS A 40 ? 1.0445 1.0926 1.0814 -0.0175 0.0140 -0.0416 39 LYS A C 311 O O . LYS A 40 ? 1.0279 1.0690 1.0608 -0.0159 0.0099 -0.0389 39 LYS A O 312 C CB . LYS A 40 ? 1.0883 1.1541 1.1292 -0.0232 0.0152 -0.0408 39 LYS A CB 313 C CG . LYS A 40 ? 1.0277 1.0896 1.0648 -0.0228 0.0104 -0.0371 39 LYS A CG 314 C CD . LYS A 40 ? 1.0618 1.1330 1.1003 -0.0259 0.0101 -0.0357 39 LYS A CD 315 C CE . LYS A 40 ? 0.9786 1.0536 1.0184 -0.0275 0.0117 -0.0358 39 LYS A CE 316 N NZ . LYS A 40 ? 1.0228 1.0959 1.0646 -0.0283 0.0096 -0.0352 39 LYS A NZ 317 N N . SER A 41 ? 0.9521 0.9976 0.9886 -0.0154 0.0173 -0.0438 40 SER A N 318 C CA . SER A 41 ? 0.8928 0.9268 0.9244 -0.0111 0.0161 -0.0432 40 SER A CA 319 C C . SER A 41 ? 0.8373 0.8658 0.8703 -0.0105 0.0147 -0.0439 40 SER A C 320 O O . SER A 41 ? 0.7253 0.7593 0.7637 -0.0133 0.0155 -0.0454 40 SER A O 321 C CB . SER A 41 ? 0.8987 0.9318 0.9293 -0.0089 0.0202 -0.0454 40 SER A CB 322 O OG . SER A 41 ? 0.8875 0.9249 0.9230 -0.0106 0.0231 -0.0476 40 SER A OG 323 N N . THR A 42 ? 0.7733 0.7908 0.8016 -0.0068 0.0126 -0.0428 41 THR A N 324 C CA . THR A 42 ? 0.6620 0.6735 0.6912 -0.0059 0.0111 -0.0432 41 THR A CA 325 C C . THR A 42 ? 0.6398 0.6446 0.6674 -0.0024 0.0135 -0.0451 41 THR A C 326 O O . THR A 42 ? 0.6941 0.6945 0.7172 0.0003 0.0143 -0.0447 41 THR A O 327 C CB . THR A 42 ? 0.6736 0.6772 0.6986 -0.0047 0.0059 -0.0400 41 THR A CB 328 O OG1 . THR A 42 ? 0.7316 0.7260 0.7499 -0.0008 0.0045 -0.0383 41 THR A OG1 329 C CG2 . THR A 42 ? 0.6483 0.6581 0.6742 -0.0077 0.0034 -0.0379 41 THR A CG2 330 N N . GLN A 43 ? 0.5850 0.5893 0.6160 -0.0027 0.0146 -0.0467 42 GLN A N 331 C CA . GLN A 43 ? 0.5834 0.5818 0.6116 0.0001 0.0148 -0.0439 42 GLN A CA 332 C C . GLN A 43 ? 0.4814 0.4698 0.5057 0.0024 0.0111 -0.0421 42 GLN A C 333 O O . GLN A 43 ? 0.4975 0.4856 0.5245 0.0009 0.0090 -0.0431 42 GLN A O 334 C CB . GLN A 43 ? 0.6707 0.6754 0.7044 -0.0020 0.0174 -0.0446 42 GLN A CB 335 C CG . GLN A 43 ? 0.8151 0.8132 0.8470 0.0000 0.0161 -0.0427 42 GLN A CG 336 C CD . GLN A 43 ? 0.9099 0.9134 0.9473 -0.0022 0.0183 -0.0434 42 GLN A CD 337 O OE1 . GLN A 43 ? 1.0080 1.0190 1.0519 -0.0057 0.0198 -0.0458 42 GLN A OE1 338 N NE2 . GLN A 43 ? 0.8968 0.8964 0.9313 -0.0003 0.0184 -0.0413 42 GLN A NE2 339 N N . THR A 44 ? 0.4874 0.4675 0.5048 0.0059 0.0100 -0.0391 43 THR A N 340 C CA . THR A 44 ? 0.4335 0.4043 0.4463 0.0079 0.0069 -0.0367 43 THR A CA 341 C C . THR A 44 ? 0.4675 0.4396 0.4832 0.0072 0.0076 -0.0366 43 THR A C 342 O O . THR A 44 ? 0.4362 0.4123 0.4536 0.0070 0.0102 -0.0367 43 THR A O 343 C CB . THR A 44 ? 0.4511 0.4133 0.4549 0.0112 0.0064 -0.0333 43 THR A CB 344 O OG1 . THR A 44 ? 0.5090 0.4702 0.5102 0.0120 0.0063 -0.0332 43 THR A OG1 345 C CG2 . THR A 44 ? 0.3650 0.3186 0.3643 0.0122 0.0041 -0.0308 43 THR A CG2 346 N N . VAL A 45 ? 0.3966 0.3652 0.4129 0.0068 0.0050 -0.0363 44 VAL A N 347 C CA . VAL A 45 ? 0.2977 0.2660 0.3157 0.0066 0.0051 -0.0358 44 VAL A CA 348 C C . VAL A 45 ? 0.3358 0.2946 0.3454 0.0094 0.0038 -0.0323 44 VAL A C 349 O O . VAL A 45 ? 0.3468 0.3045 0.3537 0.0106 0.0053 -0.0311 44 VAL A O 350 C CB . VAL A 45 ? 0.3588 0.3299 0.3829 0.0040 0.0034 -0.0375 44 VAL A CB 351 C CG1 . VAL A 45 ? 0.3076 0.2783 0.3335 0.0039 0.0037 -0.0369 44 VAL A CG1 352 C CG2 . VAL A 45 ? 0.3224 0.3034 0.3540 0.0007 0.0056 -0.0409 44 VAL A CG2 353 N N . ALA A 46 ? 0.2344 0.1867 0.2398 0.0100 0.0013 -0.0306 45 ALA A N 354 C CA . ALA A 46 ? 0.2564 0.2014 0.2556 0.0115 0.0015 -0.0274 45 ALA A CA 355 C C . ALA A 46 ? 0.3406 0.2823 0.3379 0.0120 0.0002 -0.0258 45 ALA A C 356 O O . ALA A 46 ? 0.3725 0.3151 0.3716 0.0114 -0.0030 -0.0266 45 ALA A O 357 C CB . ALA A 46 ? 0.3859 0.3296 0.3867 0.0109 0.0002 -0.0268 45 ALA A CB 358 N N . VAL A 47 ? 0.3652 0.3044 0.3605 0.0130 0.0022 -0.0237 46 VAL A N 359 C CA . VAL A 47 ? 0.3509 0.2890 0.3458 0.0139 0.0001 -0.0221 46 VAL A CA 360 C C . VAL A 47 ? 0.4226 0.3580 0.4165 0.0153 -0.0024 -0.0204 46 VAL A C 361 O O . VAL A 47 ? 0.4014 0.3366 0.3958 0.0161 -0.0009 -0.0207 46 VAL A O 362 C CB . VAL A 47 ? 0.3323 0.2717 0.3268 0.0146 0.0022 -0.0223 46 VAL A CB 363 C CG1 . VAL A 47 ? 0.2863 0.2243 0.2787 0.0154 -0.0012 -0.0209 46 VAL A CG1 364 C CG2 . VAL A 47 ? 0.3462 0.2877 0.3398 0.0139 0.0052 -0.0243 46 VAL A CG2 365 N N . HIS A 48 ? 0.3118 0.2448 0.3032 0.0158 -0.0063 -0.0185 47 HIS A N 366 C CA . HIS A 48 ? 0.3621 0.2917 0.3502 0.0172 -0.0092 -0.0168 47 HIS A CA 367 C C . HIS A 48 ? 0.3937 0.3212 0.3772 0.0183 -0.0113 -0.0151 47 HIS A C 368 O O . HIS A 48 ? 0.4347 0.3620 0.4171 0.0178 -0.0129 -0.0143 47 HIS A O 369 C CB . HIS A 48 ? 0.3459 0.2743 0.3342 0.0165 -0.0120 -0.0160 47 HIS A CB 370 C CG . HIS A 48 ? 0.3452 0.2700 0.3296 0.0176 -0.0151 -0.0144 47 HIS A CG 371 N ND1 . HIS A 48 ? 0.4481 0.3713 0.4296 0.0191 -0.0150 -0.0140 47 HIS A ND1 372 C CD2 . HIS A 48 ? 0.3802 0.3030 0.3629 0.0174 -0.0185 -0.0133 47 HIS A CD2 373 C CE1 . HIS A 48 ? 0.3844 0.3044 0.3623 0.0197 -0.0180 -0.0128 47 HIS A CE1 374 N NE2 . HIS A 48 ? 0.4447 0.3646 0.4234 0.0187 -0.0202 -0.0124 47 HIS A NE2 375 N N . HIS A 49 ? 0.3853 0.3113 0.3661 0.0197 -0.0112 -0.0146 48 HIS A N 376 C CA . HIS A 49 ? 0.4296 0.3531 0.4050 0.0208 -0.0130 -0.0131 48 HIS A CA 377 C C . HIS A 49 ? 0.4799 0.3997 0.4506 0.0218 -0.0155 -0.0119 48 HIS A C 378 O O . HIS A 49 ? 0.4336 0.3532 0.4052 0.0222 -0.0147 -0.0125 48 HIS A O 379 C CB . HIS A 49 ? 0.3392 0.2644 0.3150 0.0214 -0.0103 -0.0137 48 HIS A CB 380 C CG . HIS A 49 ? 0.5066 0.4297 0.4773 0.0224 -0.0117 -0.0123 48 HIS A CG 381 N ND1 . HIS A 49 ? 0.5221 0.4419 0.4871 0.0236 -0.0131 -0.0112 48 HIS A ND1 382 C CD2 . HIS A 49 ? 0.4126 0.3366 0.3827 0.0222 -0.0115 -0.0120 48 HIS A CD2 383 C CE1 . HIS A 49 ? 0.3939 0.3126 0.3552 0.0241 -0.0137 -0.0102 48 HIS A CE1 384 N NE2 . HIS A 49 ? 0.4043 0.3255 0.3686 0.0233 -0.0128 -0.0106 48 HIS A NE2 385 N N . PRO A 50 ? 0.4815 0.3983 0.4468 0.0222 -0.0186 -0.0104 49 PRO A N 386 C CA . PRO A 50 ? 0.4559 0.3690 0.4164 0.0229 -0.0211 -0.0096 49 PRO A CA 387 C C . PRO A 50 ? 0.4778 0.3896 0.4358 0.0242 -0.0199 -0.0098 49 PRO A C 388 O O . PRO A 50 ? 0.6023 0.5122 0.5587 0.0246 -0.0210 -0.0098 49 PRO A O 389 C CB . PRO A 50 ? 0.4960 0.4066 0.4514 0.0229 -0.0239 -0.0083 49 PRO A CB 390 C CG . PRO A 50 ? 0.4791 0.3918 0.4357 0.0228 -0.0222 -0.0083 49 PRO A CG 391 C CD . PRO A 50 ? 0.4934 0.4101 0.4569 0.0219 -0.0197 -0.0095 49 PRO A CD 392 N N . GLN A 51 ? 0.5241 0.4369 0.4817 0.0248 -0.0179 -0.0100 50 GLN A N 393 C CA . GLN A 51 ? 0.4513 0.3631 0.4066 0.0259 -0.0166 -0.0101 50 GLN A CA 394 C C . GLN A 51 ? 0.5102 0.4254 0.4711 0.0258 -0.0133 -0.0115 50 GLN A C 395 O O . GLN A 51 ? 0.4837 0.3982 0.4442 0.0264 -0.0125 -0.0118 50 GLN A O 396 C CB . GLN A 51 ? 0.5249 0.4354 0.4755 0.0267 -0.0165 -0.0093 50 GLN A CB 397 C CG . GLN A 51 ? 0.6613 0.5685 0.6062 0.0268 -0.0195 -0.0082 50 GLN A CG 398 C CD . GLN A 51 ? 0.7651 0.6689 0.7063 0.0270 -0.0221 -0.0079 50 GLN A CD 399 O OE1 . GLN A 51 ? 0.7052 0.6076 0.6451 0.0264 -0.0246 -0.0075 50 GLN A OE1 400 N NE2 . GLN A 51 ? 0.6969 0.5993 0.6362 0.0279 -0.0216 -0.0082 50 GLN A NE2 401 N N . TYR A 52 ? 0.4358 0.3546 0.4020 0.0248 -0.0112 -0.0124 51 TYR A N 402 C CA . TYR A 52 ? 0.3733 0.2955 0.3448 0.0245 -0.0079 -0.0140 51 TYR A CA 403 C C . TYR A 52 ? 0.4203 0.3443 0.3970 0.0236 -0.0067 -0.0153 51 TYR A C 404 O O . TYR A 52 ? 0.4360 0.3624 0.4165 0.0235 -0.0041 -0.0166 51 TYR A O 405 C CB . TYR A 52 ? 0.4277 0.3532 0.4021 0.0239 -0.0059 -0.0147 51 TYR A CB 406 C CG . TYR A 52 ? 0.4867 0.4106 0.4561 0.0249 -0.0065 -0.0135 51 TYR A CG 407 C CD1 . TYR A 52 ? 0.4782 0.3994 0.4429 0.0261 -0.0070 -0.0127 51 TYR A CD1 408 C CD2 . TYR A 52 ? 0.5195 0.4445 0.4889 0.0245 -0.0065 -0.0133 51 TYR A CD2 409 C CE1 . TYR A 52 ? 0.5597 0.4794 0.5196 0.0269 -0.0073 -0.0116 51 TYR A CE1 410 C CE2 . TYR A 52 ? 0.4650 0.3885 0.4299 0.0253 -0.0070 -0.0121 51 TYR A CE2 411 C CZ . TYR A 52 ? 0.5736 0.4944 0.5337 0.0265 -0.0073 -0.0113 51 TYR A CZ 412 O OH . TYR A 52 ? 0.8625 0.7817 0.8178 0.0273 -0.0075 -0.0102 51 TYR A OH 413 N N . GLY A 53 ? 0.4228 0.3460 0.3999 0.0230 -0.0086 -0.0149 52 GLY A N 414 C CA . GLY A 53 ? 0.4205 0.3450 0.4019 0.0221 -0.0076 -0.0159 52 GLY A CA 415 C C . GLY A 53 ? 0.4764 0.4044 0.4631 0.0206 -0.0054 -0.0174 52 GLY A C 416 O O . GLY A 53 ? 0.4589 0.3884 0.4461 0.0201 -0.0048 -0.0176 52 GLY A O 417 N N . PHE A 54 ? 0.4190 0.3480 0.4091 0.0198 -0.0039 -0.0184 53 PHE A N 418 C CA . PHE A 54 ? 0.3970 0.3289 0.3909 0.0182 -0.0013 -0.0199 53 PHE A CA 419 C C . PHE A 54 ? 0.3687 0.3034 0.3648 0.0178 0.0030 -0.0215 53 PHE A C 420 O O . PHE A 54 ? 0.4009 0.3359 0.3975 0.0186 0.0042 -0.0217 53 PHE A O 421 C CB . PHE A 54 ? 0.4424 0.3741 0.4380 0.0175 -0.0010 -0.0203 53 PHE A CB 422 C CG . PHE A 54 ? 0.4678 0.3969 0.4616 0.0178 -0.0050 -0.0189 53 PHE A CG 423 C CD1 . PHE A 54 ? 0.5064 0.4344 0.4980 0.0177 -0.0081 -0.0177 53 PHE A CD1 424 C CD2 . PHE A 54 ? 0.5265 0.4543 0.5206 0.0180 -0.0057 -0.0187 53 PHE A CD2 425 C CE1 . PHE A 54 ? 0.4424 0.3679 0.4319 0.0178 -0.0118 -0.0163 53 PHE A CE1 426 C CE2 . PHE A 54 ? 0.5675 0.4931 0.5599 0.0181 -0.0094 -0.0174 53 PHE A CE2 427 C CZ . PHE A 54 ? 0.5547 0.4791 0.5445 0.0180 -0.0125 -0.0162 53 PHE A CZ 428 N N . SER A 55 ? 0.3613 0.2976 0.3577 0.0165 0.0051 -0.0225 54 SER A N 429 C CA . SER A 55 ? 0.3136 0.2526 0.3087 0.0162 0.0083 -0.0231 54 SER A CA 430 C C . SER A 55 ? 0.3323 0.2719 0.3244 0.0158 0.0076 -0.0240 54 SER A C 431 O O . SER A 55 ? 0.3302 0.2697 0.3233 0.0147 0.0064 -0.0243 54 SER A O 432 C CB . SER A 55 ? 0.3688 0.3099 0.3649 0.0163 0.0091 -0.0232 54 SER A CB 433 O OG . SER A 55 ? 0.4555 0.3974 0.4463 0.0167 0.0111 -0.0231 54 SER A OG 434 N N . VAL A 56 ? 0.3454 0.2873 0.3373 0.0167 0.0074 -0.0254 55 VAL A N 435 C CA . VAL A 56 ? 0.3417 0.2896 0.3388 0.0154 0.0068 -0.0276 55 VAL A CA 436 C C . VAL A 56 ? 0.2784 0.2333 0.2793 0.0152 0.0085 -0.0292 55 VAL A C 437 O O . VAL A 56 ? 0.3177 0.2724 0.3174 0.0165 0.0094 -0.0290 55 VAL A O 438 C CB . VAL A 56 ? 0.2997 0.2490 0.3006 0.0147 0.0065 -0.0281 55 VAL A CB 439 C CG1 . VAL A 56 ? 0.2789 0.2358 0.2871 0.0123 0.0070 -0.0301 55 VAL A CG1 440 C CG2 . VAL A 56 ? 0.2035 0.1465 0.2013 0.0149 0.0052 -0.0264 55 VAL A CG2 441 N N . GLN A 57 ? 0.3395 0.3007 0.3452 0.0131 0.0093 -0.0307 56 GLN A N 442 C CA . GLN A 57 ? 0.2591 0.2265 0.2678 0.0123 0.0115 -0.0318 56 GLN A CA 443 C C . GLN A 57 ? 0.2884 0.2646 0.3051 0.0093 0.0138 -0.0338 56 GLN A C 444 O O . GLN A 57 ? 0.3820 0.3598 0.4018 0.0077 0.0133 -0.0345 56 GLN A O 445 C CB . GLN A 57 ? 0.2907 0.2574 0.2964 0.0125 0.0108 -0.0316 56 GLN A CB 446 C CG . GLN A 57 ? 0.2969 0.2580 0.2960 0.0151 0.0103 -0.0300 56 GLN A CG 447 C CD . GLN A 57 ? 0.4117 0.3648 0.4054 0.0172 0.0091 -0.0282 56 GLN A CD 448 O OE1 . GLN A 57 ? 0.5974 0.5454 0.5888 0.0169 0.0081 -0.0269 56 GLN A OE1 449 N NE2 . GLN A 57 ? 0.4972 0.4497 0.4896 0.0188 0.0097 -0.0279 56 GLN A NE2 450 N N . GLY A 58 ? 0.3328 0.3143 0.3526 0.0082 0.0163 -0.0346 57 GLY A N 451 C CA . GLY A 58 ? 0.2359 0.2258 0.2629 0.0048 0.0187 -0.0364 57 GLY A CA 452 C C . GLY A 58 ? 0.3075 0.2986 0.3386 0.0036 0.0193 -0.0369 57 GLY A C 453 O O . GLY A 58 ? 0.3625 0.3496 0.3917 0.0052 0.0188 -0.0361 57 GLY A O 454 N N . ASP A 59 ? 0.3117 0.3086 0.3485 0.0006 0.0204 -0.0384 58 ASP A N 455 C CA . ASP A 59 ? 0.3411 0.3397 0.3824 -0.0009 0.0211 -0.0390 58 ASP A CA 456 C C . ASP A 59 ? 0.3990 0.3930 0.4384 0.0007 0.0187 -0.0382 58 ASP A C 457 O O . ASP A 59 ? 0.3882 0.3837 0.4314 -0.0006 0.0191 -0.0387 58 ASP A O 458 C CB . ASP A 59 ? 0.4427 0.4489 0.4905 -0.0050 0.0231 -0.0409 58 ASP A CB 459 C CG . ASP A 59 ? 0.5521 0.5614 0.6030 -0.0067 0.0227 -0.0425 58 ASP A CG 460 O OD1 . ASP A 59 ? 0.5532 0.5595 0.6010 -0.0049 0.0212 -0.0424 58 ASP A OD1 461 O OD2 . ASP A 59 ? 0.5838 0.5987 0.6411 -0.0103 0.0240 -0.0446 58 ASP A OD2 462 N N . TYR A 60 ? 0.3092 0.2970 0.3425 0.0031 0.0161 -0.0369 59 TYR A N 463 C CA . TYR A 60 ? 0.2809 0.2627 0.3115 0.0044 0.0134 -0.0360 59 TYR A CA 464 C C . TYR A 60 ? 0.3090 0.2852 0.3360 0.0067 0.0126 -0.0345 59 TYR A C 465 O O . TYR A 60 ? 0.3372 0.3093 0.3629 0.0074 0.0108 -0.0338 59 TYR A O 466 C CB . TYR A 60 ? 0.2835 0.2614 0.3114 0.0050 0.0111 -0.0360 59 TYR A CB 467 C CG . TYR A 60 ? 0.2741 0.2591 0.3094 0.0019 0.0121 -0.0389 59 TYR A CG 468 C CD1 . TYR A 60 ? 0.2516 0.2390 0.2924 -0.0001 0.0114 -0.0402 59 TYR A CD1 469 C CD2 . TYR A 60 ? 0.2833 0.2732 0.3201 0.0008 0.0139 -0.0402 59 TYR A CD2 470 C CE1 . TYR A 60 ? 0.3187 0.3128 0.3658 -0.0031 0.0124 -0.0429 59 TYR A CE1 471 C CE2 . TYR A 60 ? 0.2742 0.2713 0.3174 -0.0024 0.0150 -0.0430 59 TYR A CE2 472 C CZ . TYR A 60 ? 0.3290 0.3281 0.3771 -0.0043 0.0142 -0.0444 59 TYR A CZ 473 O OH . TYR A 60 ? 0.3460 0.3522 0.3997 -0.0076 0.0151 -0.0471 59 TYR A OH 474 N N . GLN A 61 ? 0.2499 0.2258 0.2753 0.0079 0.0138 -0.0343 60 GLN A N 475 C CA . GLN A 61 ? 0.2726 0.2433 0.2943 0.0100 0.0131 -0.0331 60 GLN A CA 476 C C . GLN A 61 ? 0.3764 0.3489 0.4025 0.0090 0.0138 -0.0335 60 GLN A C 477 O O . GLN A 61 ? 0.3848 0.3638 0.4174 0.0066 0.0162 -0.0349 60 GLN A O 478 C CB . GLN A 61 ? 0.2285 0.1999 0.2490 0.0109 0.0146 -0.0330 60 GLN A CB 479 C CG . GLN A 61 ? 0.1959 0.1659 0.2125 0.0119 0.0142 -0.0325 60 GLN A CG 480 C CD . GLN A 61 ? 0.3073 0.2756 0.3208 0.0136 0.0149 -0.0319 60 GLN A CD 481 O OE1 . GLN A 61 ? 0.3422 0.3148 0.3579 0.0126 0.0168 -0.0326 60 GLN A OE1 482 N NE2 . GLN A 61 ? 0.2079 0.1698 0.2163 0.0161 0.0133 -0.0306 60 GLN A NE2 483 N N . GLY A 62 ? 0.3723 0.3387 0.3945 0.0109 0.0118 -0.0323 61 GLY A N 484 C CA . GLY A 62 ? 0.2675 0.2349 0.2933 0.0101 0.0121 -0.0325 61 GLY A CA 485 C C . GLY A 62 ? 0.3492 0.3188 0.3788 0.0083 0.0114 -0.0331 61 GLY A C 486 O O . GLY A 62 ? 0.3874 0.3579 0.4202 0.0076 0.0116 -0.0333 61 GLY A O 487 N N . ARG A 63 ? 0.2916 0.2620 0.3210 0.0075 0.0107 -0.0334 62 ARG A N 488 C CA . ARG A 63 ? 0.3152 0.2875 0.3479 0.0057 0.0098 -0.0339 62 ARG A CA 489 C C . ARG A 63 ? 0.3679 0.3342 0.3954 0.0064 0.0066 -0.0325 62 ARG A C 490 O O . ARG A 63 ? 0.3283 0.2962 0.3595 0.0047 0.0056 -0.0332 62 ARG A O 491 C CB . ARG A 63 ? 0.2417 0.2224 0.2807 0.0030 0.0124 -0.0358 62 ARG A CB 492 C CG . ARG A 63 ? 0.3059 0.2923 0.3499 0.0017 0.0157 -0.0369 62 ARG A CG 493 C CD . ARG A 63 ? 0.2928 0.2868 0.3420 -0.0012 0.0182 -0.0386 62 ARG A CD 494 N NE . ARG A 63 ? 0.3600 0.3574 0.4142 -0.0032 0.0181 -0.0401 62 ARG A NE 495 C CZ . ARG A 63 ? 0.3281 0.3285 0.3845 -0.0046 0.0183 -0.0417 62 ARG A CZ 496 N NH1 . ARG A 63 ? 0.3571 0.3574 0.4102 -0.0040 0.0185 -0.0416 62 ARG A NH1 497 N NH2 . ARG A 63 ? 0.3636 0.3676 0.4257 -0.0066 0.0182 -0.0435 62 ARG A NH2 498 N N . VAL A 64 ? 0.2781 0.2380 0.2986 0.0085 0.0052 -0.0310 63 VAL A N 499 C CA . VAL A 64 ? 0.3428 0.2972 0.3585 0.0087 0.0027 -0.0296 63 VAL A CA 500 C C . VAL A 64 ? 0.4139 0.3610 0.4242 0.0105 0.0014 -0.0276 63 VAL A C 501 O O . VAL A 64 ? 0.3761 0.3212 0.3837 0.0122 0.0025 -0.0271 63 VAL A O 502 C CB . VAL A 64 ? 0.2822 0.2367 0.2952 0.0089 0.0029 -0.0297 63 VAL A CB 503 C CG1 . VAL A 64 ? 0.2435 0.1925 0.2527 0.0092 0.0007 -0.0283 63 VAL A CG1 504 C CG2 . VAL A 64 ? 0.2946 0.2580 0.3167 0.0065 0.0042 -0.0328 63 VAL A CG2 505 N N . LEU A 65 ? 0.3574 0.3014 0.3669 0.0099 -0.0006 -0.0264 64 LEU A N 506 C CA . LEU A 65 ? 0.3647 0.3034 0.3710 0.0111 -0.0017 -0.0246 64 LEU A CA 507 C C . LEU A 65 ? 0.3976 0.3345 0.4029 0.0106 -0.0039 -0.0234 64 LEU A C 508 O O . LEU A 65 ? 0.3435 0.2822 0.3507 0.0089 -0.0052 -0.0237 64 LEU A O 509 C CB . LEU A 65 ? 0.4283 0.3665 0.4367 0.0110 -0.0027 -0.0242 64 LEU A CB 510 C CG . LEU A 65 ? 0.4442 0.3845 0.4548 0.0114 -0.0011 -0.0253 64 LEU A CG 511 C CD1 . LEU A 65 ? 0.3943 0.3338 0.4071 0.0109 -0.0025 -0.0247 64 LEU A CD1 512 C CD2 . LEU A 65 ? 0.3656 0.3037 0.3728 0.0133 0.0006 -0.0249 64 LEU A CD2 513 N N . PHE A 66 ? 0.4431 0.3773 0.4460 0.0120 -0.0046 -0.0220 65 PHE A N 514 C CA . PHE A 66 ? 0.3929 0.3257 0.3950 0.0120 -0.0079 -0.0206 65 PHE A CA 515 C C . PHE A 66 ? 0.5339 0.4650 0.5364 0.0120 -0.0109 -0.0194 65 PHE A C 516 O O . PHE A 66 ? 0.5556 0.4855 0.5579 0.0129 -0.0107 -0.0192 65 PHE A O 517 C CB . PHE A 66 ? 0.4616 0.3926 0.4607 0.0136 -0.0085 -0.0195 65 PHE A CB 518 C CG . PHE A 66 ? 0.4962 0.4286 0.4948 0.0132 -0.0073 -0.0200 65 PHE A CG 519 C CD1 . PHE A 66 ? 0.4198 0.3525 0.4182 0.0122 -0.0096 -0.0194 65 PHE A CD1 520 C CD2 . PHE A 66 ? 0.4396 0.3732 0.4378 0.0137 -0.0040 -0.0210 65 PHE A CD2 521 C CE1 . PHE A 66 ? 0.4538 0.3876 0.4518 0.0119 -0.0090 -0.0201 65 PHE A CE1 522 C CE2 . PHE A 66 ? 0.4234 0.3584 0.4211 0.0133 -0.0029 -0.0215 65 PHE A CE2 523 C CZ . PHE A 66 ? 0.4254 0.3606 0.4230 0.0123 -0.0051 -0.0211 65 PHE A CZ 524 N N . LYS A 67 ? 0.6058 0.5370 0.6090 0.0109 -0.0137 -0.0186 66 LYS A N 525 C CA . LYS A 67 ? 0.6290 0.5587 0.6324 0.0109 -0.0168 -0.0175 66 LYS A CA 526 C C . LYS A 67 ? 0.6906 0.6169 0.6901 0.0127 -0.0193 -0.0158 66 LYS A C 527 O O . LYS A 67 ? 0.6476 0.5724 0.6468 0.0132 -0.0202 -0.0154 66 LYS A O 528 C CB . LYS A 67 ? 0.5911 0.5216 0.5958 0.0093 -0.0194 -0.0168 66 LYS A CB 529 C CG . LYS A 67 ? 0.5987 0.5279 0.6037 0.0091 -0.0226 -0.0156 66 LYS A CG 530 C CD . LYS A 67 ? 0.6932 0.6228 0.6990 0.0077 -0.0261 -0.0147 66 LYS A CD 531 C CE . LYS A 67 ? 0.6683 0.5965 0.6737 0.0076 -0.0292 -0.0131 66 LYS A CE 532 N NZ . LYS A 67 ? 0.7070 0.6367 0.7162 0.0069 -0.0278 -0.0140 66 LYS A NZ 533 N N . ASN A 68 ? 0.6797 0.6047 0.6758 0.0135 -0.0204 -0.0150 67 ASN A N 534 C CA . ASN A 68 ? 0.7487 0.6703 0.7402 0.0149 -0.0231 -0.0136 67 ASN A CA 535 C C . ASN A 68 ? 0.6657 0.5864 0.6538 0.0161 -0.0225 -0.0133 67 ASN A C 536 O O . ASN A 68 ? 0.6606 0.5832 0.6501 0.0158 -0.0201 -0.0141 67 ASN A O 537 C CB . ASN A 68 ? 0.6987 0.6185 0.6882 0.0144 -0.0275 -0.0121 67 ASN A CB 538 C CG . ASN A 68 ? 0.6875 0.6085 0.6774 0.0133 -0.0288 -0.0116 67 ASN A CG 539 O OD1 . ASN A 68 ? 0.7241 0.6455 0.7128 0.0136 -0.0277 -0.0117 67 ASN A OD1 540 N ND2 . ASN A 68 ? 0.7127 0.6342 0.7043 0.0121 -0.0310 -0.0110 67 ASN A ND2 541 N N . TYR A 69 ? 0.6389 0.5565 0.6223 0.0173 -0.0248 -0.0122 68 TYR A N 542 C CA . TYR A 69 ? 0.7044 0.6206 0.6836 0.0184 -0.0248 -0.0118 68 TYR A CA 543 C C . TYR A 69 ? 0.7112 0.6262 0.6871 0.0181 -0.0276 -0.0106 68 TYR A C 544 O O . TYR A 69 ? 0.6019 0.5157 0.5742 0.0189 -0.0276 -0.0102 68 TYR A O 545 C CB . TYR A 69 ? 0.7124 0.6257 0.6877 0.0197 -0.0257 -0.0114 68 TYR A CB 546 C CG . TYR A 69 ? 0.7571 0.6716 0.7351 0.0203 -0.0225 -0.0125 68 TYR A CG 547 C CD1 . TYR A 69 ? 0.7425 0.6579 0.7203 0.0210 -0.0198 -0.0131 68 TYR A CD1 548 C CD2 . TYR A 69 ? 0.7748 0.6897 0.7555 0.0200 -0.0221 -0.0130 68 TYR A CD2 549 C CE1 . TYR A 69 ? 0.8534 0.7700 0.8338 0.0214 -0.0168 -0.0141 68 TYR A CE1 550 C CE2 . TYR A 69 ? 0.8481 0.7640 0.8313 0.0204 -0.0190 -0.0140 68 TYR A CE2 551 C CZ . TYR A 69 ? 0.8514 0.7683 0.8344 0.0211 -0.0164 -0.0146 68 TYR A CZ 552 O OH . TYR A 69 ? 0.7487 0.6667 0.7342 0.0215 -0.0133 -0.0156 68 TYR A OH 553 N N . SER A 70 ? 0.6269 0.5421 0.6037 0.0169 -0.0299 -0.0100 69 SER A N 554 C CA . SER A 70 ? 0.5806 0.4947 0.5544 0.0165 -0.0325 -0.0088 69 SER A CA 555 C C . SER A 70 ? 0.6172 0.5337 0.5929 0.0161 -0.0305 -0.0092 69 SER A C 556 O O . SER A 70 ? 0.6512 0.5706 0.6317 0.0151 -0.0285 -0.0101 69 SER A O 557 C CB . SER A 70 ? 0.5616 0.4756 0.5363 0.0153 -0.0356 -0.0081 69 SER A CB 558 O OG . SER A 70 ? 0.5525 0.4663 0.5254 0.0146 -0.0375 -0.0072 69 SER A OG 559 N N . LEU A 71 ? 0.6235 0.5386 0.5951 0.0168 -0.0311 -0.0085 70 LEU A N 560 C CA . LEU A 71 ? 0.5975 0.5146 0.5705 0.0164 -0.0294 -0.0086 70 LEU A CA 561 C C . LEU A 71 ? 0.6029 0.5216 0.5783 0.0149 -0.0307 -0.0082 70 LEU A C 562 O O . LEU A 71 ? 0.6824 0.6030 0.6599 0.0143 -0.0293 -0.0088 70 LEU A O 563 C CB . LEU A 71 ? 0.5641 0.4791 0.5319 0.0174 -0.0301 -0.0078 70 LEU A CB 564 C CG . LEU A 71 ? 0.5324 0.4474 0.4991 0.0187 -0.0273 -0.0084 70 LEU A CG 565 C CD1 . LEU A 71 ? 0.4586 0.3773 0.4304 0.0184 -0.0236 -0.0098 70 LEU A CD1 566 C CD2 . LEU A 71 ? 0.6013 0.5147 0.5669 0.0196 -0.0273 -0.0088 70 LEU A CD2 567 N N . ASN A 72 ? 0.5720 0.4895 0.5467 0.0141 -0.0338 -0.0074 71 ASN A N 568 C CA . ASN A 72 ? 0.6932 0.6117 0.6698 0.0126 -0.0360 -0.0070 71 ASN A CA 569 C C . ASN A 72 ? 0.6394 0.5596 0.6210 0.0116 -0.0360 -0.0082 71 ASN A C 570 O O . ASN A 72 ? 0.5434 0.4640 0.5268 0.0102 -0.0389 -0.0081 71 ASN A O 571 C CB . ASN A 72 ? 0.7113 0.6278 0.6845 0.0122 -0.0396 -0.0054 71 ASN A CB 572 C CG . ASN A 72 ? 0.7274 0.6418 0.6956 0.0127 -0.0409 -0.0045 71 ASN A CG 573 O OD1 . ASN A 72 ? 0.7640 0.6762 0.7283 0.0140 -0.0406 -0.0046 71 ASN A OD1 574 N ND2 . ASN A 72 ? 0.8460 0.7605 0.8136 0.0118 -0.0430 -0.0038 71 ASN A ND2 575 N N . ASP A 73 ? 0.6053 0.5269 0.5895 0.0119 -0.0326 -0.0094 72 ASP A N 576 C CA . ASP A 73 ? 0.6712 0.5948 0.6604 0.0109 -0.0317 -0.0109 72 ASP A CA 577 C C . ASP A 73 ? 0.5785 0.5043 0.5703 0.0111 -0.0275 -0.0130 72 ASP A C 578 O O . ASP A 73 ? 0.6288 0.5549 0.6204 0.0120 -0.0240 -0.0133 72 ASP A O 579 C CB . ASP A 73 ? 0.6780 0.6013 0.6679 0.0110 -0.0314 -0.0105 72 ASP A CB 580 C CG . ASP A 73 ? 0.6705 0.5955 0.6650 0.0096 -0.0321 -0.0115 72 ASP A CG 581 O OD1 . ASP A 73 ? 0.5766 0.5037 0.5746 0.0085 -0.0317 -0.0130 72 ASP A OD1 582 O OD2 . ASP A 73 ? 0.6677 0.5922 0.6626 0.0094 -0.0328 -0.0108 72 ASP A OD2 583 N N . ALA A 74 ? 0.4938 0.4213 0.4881 0.0100 -0.0278 -0.0145 73 ALA A N 584 C CA . ALA A 74 ? 0.5264 0.4565 0.5233 0.0099 -0.0239 -0.0169 73 ALA A CA 585 C C . ALA A 74 ? 0.5178 0.4509 0.5200 0.0085 -0.0222 -0.0191 73 ALA A C 586 O O . ALA A 74 ? 0.5497 0.4857 0.5545 0.0079 -0.0191 -0.0214 73 ALA A O 587 C CB . ALA A 74 ? 0.4854 0.4163 0.4823 0.0095 -0.0247 -0.0179 73 ALA A CB 588 N N . THR A 75 ? 0.5224 0.4552 0.5261 0.0077 -0.0241 -0.0183 74 THR A N 589 C CA . THR A 75 ? 0.4188 0.3548 0.4278 0.0061 -0.0230 -0.0201 74 THR A CA 590 C C . THR A 75 ? 0.3944 0.3313 0.4037 0.0068 -0.0183 -0.0214 74 THR A C 591 O O . THR A 75 ? 0.4346 0.3690 0.4404 0.0084 -0.0166 -0.0200 74 THR A O 592 C CB . THR A 75 ? 0.5189 0.4537 0.5287 0.0055 -0.0260 -0.0186 74 THR A CB 593 O OG1 . THR A 75 ? 0.5875 0.5218 0.5971 0.0045 -0.0303 -0.0174 74 THR A OG1 594 C CG2 . THR A 75 ? 0.4170 0.3552 0.4324 0.0038 -0.0246 -0.0203 74 THR A CG2 595 N N . ILE A 76 ? 0.4023 0.3434 0.4160 0.0054 -0.0161 -0.0240 75 ILE A N 596 C CA . ILE A 76 ? 0.3601 0.3027 0.3743 0.0059 -0.0120 -0.0252 75 ILE A CA 597 C C . ILE A 76 ? 0.3849 0.3314 0.4050 0.0040 -0.0118 -0.0267 75 ILE A C 598 O O . ILE A 76 ? 0.3891 0.3384 0.4139 0.0020 -0.0141 -0.0273 75 ILE A O 599 C CB . ILE A 76 ? 0.3391 0.2843 0.3532 0.0061 -0.0091 -0.0270 75 ILE A CB 600 C CG1 . ILE A 76 ? 0.3189 0.2703 0.3397 0.0037 -0.0097 -0.0297 75 ILE A CG1 601 C CG2 . ILE A 76 ? 0.3451 0.2867 0.3538 0.0078 -0.0091 -0.0254 75 ILE A CG2 602 C CD1 . ILE A 76 ? 0.3473 0.3030 0.3694 0.0037 -0.0067 -0.0319 75 ILE A CD1 603 N N . THR A 77 ? 0.3907 0.3378 0.4106 0.0047 -0.0089 -0.0270 76 THR A N 604 C CA . THR A 77 ? 0.3653 0.3175 0.3918 0.0031 -0.0079 -0.0287 76 THR A CA 605 C C . THR A 77 ? 0.3808 0.3378 0.4096 0.0032 -0.0041 -0.0307 76 THR A C 606 O O . THR A 77 ? 0.3548 0.3093 0.3783 0.0051 -0.0024 -0.0299 76 THR A O 607 C CB . THR A 77 ? 0.4150 0.3646 0.4405 0.0035 -0.0083 -0.0273 76 THR A CB 608 O OG1 . THR A 77 ? 0.4806 0.4259 0.4996 0.0057 -0.0064 -0.0258 76 THR A OG1 609 C CG2 . THR A 77 ? 0.3820 0.3285 0.4068 0.0031 -0.0119 -0.0256 76 THR A CG2 610 N N . LEU A 78 ? 0.4721 0.4365 0.5091 0.0009 -0.0027 -0.0332 77 LEU A N 611 C CA . LEU A 78 ? 0.3412 0.3126 0.3827 0.0002 0.0013 -0.0354 77 LEU A CA 612 C C . LEU A 78 ? 0.3073 0.2831 0.3545 -0.0009 0.0033 -0.0363 77 LEU A C 613 O O . LEU A 78 ? 0.3420 0.3189 0.3931 -0.0024 0.0021 -0.0364 77 LEU A O 614 C CB . LEU A 78 ? 0.3350 0.3127 0.3816 -0.0022 0.0021 -0.0378 77 LEU A CB 615 C CG . LEU A 78 ? 0.4081 0.3939 0.4596 -0.0034 0.0067 -0.0402 77 LEU A CG 616 C CD1 . LEU A 78 ? 0.3197 0.3029 0.3656 -0.0010 0.0080 -0.0391 77 LEU A CD1 617 C CD2 . LEU A 78 ? 0.4263 0.4177 0.4817 -0.0059 0.0072 -0.0424 77 LEU A CD2 618 N N . HIS A 79 ? 0.3890 0.3671 0.4363 -0.0002 0.0063 -0.0365 78 HIS A N 619 C CA . HIS A 79 ? 0.3503 0.3311 0.4014 -0.0007 0.0080 -0.0367 78 HIS A CA 620 C C . HIS A 79 ? 0.3374 0.3265 0.3944 -0.0024 0.0123 -0.0387 78 HIS A C 621 O O . HIS A 79 ? 0.3112 0.3023 0.3671 -0.0025 0.0137 -0.0393 78 HIS A O 622 C CB . HIS A 79 ? 0.3841 0.3580 0.4277 0.0019 0.0068 -0.0342 78 HIS A CB 623 C CG . HIS A 79 ? 0.3553 0.3210 0.3925 0.0033 0.0031 -0.0320 78 HIS A CG 624 N ND1 . HIS A 79 ? 0.4375 0.4006 0.4745 0.0033 0.0016 -0.0308 78 HIS A ND1 625 C CD2 . HIS A 79 ? 0.3918 0.3519 0.4228 0.0044 0.0008 -0.0306 78 HIS A CD2 626 C CE1 . HIS A 79 ? 0.3332 0.2896 0.3645 0.0043 -0.0012 -0.0290 78 HIS A CE1 627 N NE2 . HIS A 79 ? 0.3879 0.3423 0.4152 0.0049 -0.0016 -0.0287 78 HIS A NE2 628 N N . ASN A 80 ? 0.3169 0.3105 0.3797 -0.0038 0.0144 -0.0395 79 ASN A N 629 C CA . ASN A 80 ? 0.3649 0.3669 0.4343 -0.0065 0.0186 -0.0414 79 ASN A CA 630 C C . ASN A 80 ? 0.3801 0.3878 0.4534 -0.0086 0.0201 -0.0437 79 ASN A C 631 O O . ASN A 80 ? 0.3857 0.3959 0.4582 -0.0095 0.0216 -0.0441 79 ASN A O 632 C CB . ASN A 80 ? 0.3499 0.3509 0.4153 -0.0056 0.0198 -0.0402 79 ASN A CB 633 C CG . ASN A 80 ? 0.4528 0.4512 0.5179 -0.0046 0.0197 -0.0392 79 ASN A CG 634 O OD1 . ASN A 80 ? 0.4742 0.4675 0.5346 -0.0023 0.0185 -0.0380 79 ASN A OD1 635 N ND2 . ASN A 80 ? 0.3497 0.3521 0.4207 -0.0066 0.0212 -0.0399 79 ASN A ND2 636 N N . ILE A 81 ? 0.3428 0.3523 0.4197 -0.0095 0.0193 -0.0448 80 ILE A N 637 C CA . ILE A 81 ? 0.3048 0.3185 0.3835 -0.0109 0.0201 -0.0467 80 ILE A CA 638 C C . ILE A 81 ? 0.3813 0.4020 0.4626 -0.0132 0.0239 -0.0481 80 ILE A C 639 O O . ILE A 81 ? 0.3289 0.3497 0.4091 -0.0136 0.0248 -0.0473 80 ILE A O 640 C CB . ILE A 81 ? 0.3342 0.3461 0.4131 -0.0112 0.0173 -0.0465 80 ILE A CB 641 C CG1 . ILE A 81 ? 0.3637 0.3665 0.4357 -0.0096 0.0121 -0.0440 80 ILE A CG1 642 C CG2 . ILE A 81 ? 0.3044 0.3219 0.3850 -0.0131 0.0189 -0.0484 80 ILE A CG2 643 C CD1 . ILE A 81 ? 0.4511 0.4506 0.5225 -0.0103 0.0081 -0.0425 80 ILE A CD1 644 N N . GLY A 82 ? 0.3251 0.3472 0.4035 -0.0140 0.0243 -0.0485 81 GLY A N 645 C CA . GLY A 82 ? 0.2411 0.2641 0.3150 -0.0160 0.0250 -0.0480 81 GLY A CA 646 C C . GLY A 82 ? 0.2774 0.2993 0.3464 -0.0153 0.0254 -0.0507 81 GLY A C 647 O O . GLY A 82 ? 0.3948 0.4200 0.4676 -0.0150 0.0251 -0.0513 81 GLY A O 648 N N . PHE A 83 ? 0.2650 0.2875 0.3308 -0.0172 0.0259 -0.0513 82 PHE A N 649 C CA . PHE A 83 ? 0.2365 0.2625 0.3011 -0.0183 0.0264 -0.0528 82 PHE A CA 650 C C . PHE A 83 ? 0.2511 0.2784 0.3151 -0.0183 0.0259 -0.0532 82 PHE A C 651 O O . PHE A 83 ? 0.3177 0.3480 0.3828 -0.0187 0.0258 -0.0544 82 PHE A O 652 C CB . PHE A 83 ? 0.2434 0.2701 0.3047 -0.0197 0.0271 -0.0530 82 PHE A CB 653 C CG . PHE A 83 ? 0.3203 0.3467 0.3821 -0.0199 0.0278 -0.0533 82 PHE A CG 654 C CD1 . PHE A 83 ? 0.3246 0.3532 0.3883 -0.0204 0.0281 -0.0545 82 PHE A CD1 655 C CD2 . PHE A 83 ? 0.3157 0.3398 0.3763 -0.0200 0.0280 -0.0522 82 PHE A CD2 656 C CE1 . PHE A 83 ? 0.2740 0.3023 0.3384 -0.0208 0.0288 -0.0548 82 PHE A CE1 657 C CE2 . PHE A 83 ? 0.2864 0.3104 0.3482 -0.0204 0.0289 -0.0532 82 PHE A CE2 658 C CZ . PHE A 83 ? 0.3091 0.3352 0.3728 -0.0208 0.0294 -0.0545 82 PHE A CZ 659 N N . SER A 84 ? 0.3308 0.3563 0.3939 -0.0183 0.0253 -0.0520 83 SER A N 660 C CA . SER A 84 ? 0.3021 0.3292 0.3648 -0.0185 0.0248 -0.0522 83 SER A CA 661 C C . SER A 84 ? 0.3860 0.4131 0.4520 -0.0172 0.0238 -0.0525 83 SER A C 662 O O . SER A 84 ? 0.3188 0.3488 0.3850 -0.0164 0.0242 -0.0529 83 SER A O 663 C CB . SER A 84 ? 0.2400 0.2666 0.3022 -0.0187 0.0251 -0.0509 83 SER A CB 664 O OG . SER A 84 ? 0.3941 0.4189 0.4592 -0.0176 0.0252 -0.0496 83 SER A OG 665 N N . ASP A 85 ? 0.3267 0.3549 0.3982 -0.0156 0.0241 -0.0518 84 ASP A N 666 C CA . ASP A 85 ? 0.3878 0.4128 0.4606 -0.0146 0.0213 -0.0519 84 ASP A CA 667 C C . ASP A 85 ? 0.3159 0.3420 0.3870 -0.0164 0.0187 -0.0513 84 ASP A C 668 O O . ASP A 85 ? 0.3696 0.3911 0.4381 -0.0164 0.0142 -0.0494 84 ASP A O 669 C CB . ASP A 85 ? 0.2964 0.3152 0.3686 -0.0130 0.0189 -0.0499 84 ASP A CB 670 C CG . ASP A 85 ? 0.3150 0.3298 0.3845 -0.0111 0.0194 -0.0483 84 ASP A CG 671 O OD1 . ASP A 85 ? 0.3720 0.3848 0.4371 -0.0100 0.0194 -0.0475 84 ASP A OD1 672 O OD2 . ASP A 85 ? 0.3375 0.3511 0.4083 -0.0106 0.0196 -0.0474 84 ASP A OD2 673 N N . SER A 86 ? 0.2897 0.3204 0.3602 -0.0179 0.0206 -0.0519 85 SER A N 674 C CA . SER A 86 ? 0.3634 0.3969 0.4321 -0.0200 0.0180 -0.0494 85 SER A CA 675 C C . SER A 86 ? 0.3531 0.3886 0.4196 -0.0206 0.0170 -0.0490 85 SER A C 676 O O . SER A 86 ? 0.4020 0.4382 0.4675 -0.0199 0.0195 -0.0512 85 SER A O 677 C CB . SER A 86 ? 0.3531 0.3898 0.4202 -0.0211 0.0199 -0.0493 85 SER A CB 678 O OG . SER A 86 ? 0.5271 0.5672 0.5927 -0.0229 0.0178 -0.0467 85 SER A OG 679 N N . GLY A 87 ? 0.3337 0.3697 0.3992 -0.0220 0.0133 -0.0464 86 GLY A N 680 C CA . GLY A 87 ? 0.3536 0.3921 0.4171 -0.0228 0.0123 -0.0458 86 GLY A CA 681 C C . GLY A 87 ? 0.3994 0.4337 0.4618 -0.0230 0.0072 -0.0439 86 GLY A C 682 O O . GLY A 87 ? 0.3290 0.3590 0.3917 -0.0229 0.0042 -0.0425 86 GLY A O 683 N N . LYS A 88 ? 0.4437 0.4786 0.5041 -0.0231 0.0062 -0.0439 87 LYS A N 684 C CA . LYS A 88 ? 0.4082 0.4386 0.4661 -0.0232 0.0012 -0.0422 87 LYS A CA 685 C C . LYS A 88 ? 0.3724 0.3937 0.4255 -0.0197 0.0002 -0.0425 87 LYS A C 686 O O . LYS A 88 ? 0.4387 0.4607 0.4903 -0.0183 0.0032 -0.0438 87 LYS A O 687 C CB . LYS A 88 ? 0.4537 0.4900 0.5103 -0.0249 0.0003 -0.0404 87 LYS A CB 688 C CG . LYS A 88 ? 0.6163 0.6489 0.6709 -0.0254 -0.0052 -0.0379 87 LYS A CG 689 C CD . LYS A 88 ? 0.6271 0.6628 0.6791 -0.0260 -0.0065 -0.0364 87 LYS A CD 690 C CE . LYS A 88 ? 0.7534 0.7945 0.8059 -0.0282 -0.0079 -0.0335 87 LYS A CE 691 N NZ . LYS A 88 ? 0.8285 0.8740 0.8790 -0.0290 -0.0083 -0.0323 87 LYS A NZ 692 N N . TYR A 89 ? 0.3947 0.4070 0.4443 -0.0176 -0.0038 -0.0403 88 TYR A N 693 C CA . TYR A 89 ? 0.3740 0.3760 0.4172 -0.0135 -0.0053 -0.0392 88 TYR A CA 694 C C . TYR A 89 ? 0.4245 0.4223 0.4624 -0.0127 -0.0098 -0.0358 88 TYR A C 695 O O . TYR A 89 ? 0.4470 0.4480 0.4863 -0.0151 -0.0124 -0.0342 88 TYR A O 696 C CB . TYR A 89 ? 0.3772 0.3713 0.4203 -0.0115 -0.0063 -0.0396 88 TYR A CB 697 C CG . TYR A 89 ? 0.3736 0.3702 0.4213 -0.0117 -0.0019 -0.0428 88 TYR A CG 698 C CD1 . TYR A 89 ? 0.3040 0.3086 0.3585 -0.0151 0.0001 -0.0444 88 TYR A CD1 699 C CD2 . TYR A 89 ? 0.3869 0.3776 0.4319 -0.0083 0.0001 -0.0438 88 TYR A CD2 700 C CE1 . TYR A 89 ? 0.4076 0.4148 0.4651 -0.0146 0.0042 -0.0459 88 TYR A CE1 701 C CE2 . TYR A 89 ? 0.4337 0.4277 0.4818 -0.0080 0.0040 -0.0448 88 TYR A CE2 702 C CZ . TYR A 89 ? 0.4125 0.4146 0.4672 -0.0111 0.0061 -0.0463 88 TYR A CZ 703 O OH . TYR A 89 ? 0.3217 0.3271 0.3797 -0.0108 0.0099 -0.0473 88 TYR A OH 704 N N . ILE A 90 ? 0.3565 0.3467 0.3883 -0.0093 -0.0106 -0.0347 89 ILE A N 705 C CA . ILE A 90 ? 0.4023 0.3869 0.4285 -0.0081 -0.0149 -0.0313 89 ILE A CA 706 C C . ILE A 90 ? 0.4274 0.3998 0.4482 -0.0042 -0.0169 -0.0304 89 ILE A C 707 O O . ILE A 90 ? 0.3954 0.3640 0.4142 -0.0016 -0.0144 -0.0318 89 ILE A O 708 C CB . ILE A 90 ? 0.3905 0.3789 0.4140 -0.0082 -0.0142 -0.0304 89 ILE A CB 709 C CG1 . ILE A 90 ? 0.4732 0.4607 0.4949 -0.0060 -0.0105 -0.0321 89 ILE A CG1 710 C CG2 . ILE A 90 ? 0.3971 0.3975 0.4258 -0.0123 -0.0128 -0.0309 89 ILE A CG2 711 C CD1 . ILE A 90 ? 0.5994 0.5851 0.6159 -0.0045 -0.0112 -0.0301 89 ILE A CD1 712 N N . CYS A 91 ? 0.4420 0.4082 0.4604 -0.0037 -0.0213 -0.0281 90 CYS A N 713 C CA . CYS A 91 ? 0.4336 0.3881 0.4457 -0.0001 -0.0238 -0.0265 90 CYS A CA 714 C C . CYS A 91 ? 0.4607 0.4126 0.4670 0.0013 -0.0252 -0.0242 90 CYS A C 715 O O . CYS A 91 ? 0.6069 0.5639 0.6135 -0.0007 -0.0266 -0.0227 90 CYS A O 716 C CB . CYS A 91 ? 0.3851 0.3340 0.3967 -0.0003 -0.0281 -0.0248 90 CYS A CB 717 S SG . CYS A 91 ? 0.5393 0.4776 0.5439 0.0040 -0.0290 -0.0222 90 CYS A SG 718 N N . LYS A 92 ? 0.4680 0.4120 0.4690 0.0048 -0.0247 -0.0240 91 LYS A N 719 C CA . LYS A 92 ? 0.4197 0.3614 0.4153 0.0063 -0.0254 -0.0221 91 LYS A CA 720 C C . LYS A 92 ? 0.4237 0.3547 0.4126 0.0099 -0.0271 -0.0199 91 LYS A C 721 O O . LYS A 92 ? 0.4883 0.4193 0.4769 0.0115 -0.0237 -0.0198 91 LYS A O 722 C CB . LYS A 92 ? 0.4353 0.3834 0.4324 0.0062 -0.0209 -0.0240 91 LYS A CB 723 C CG . LYS A 92 ? 0.4952 0.4423 0.4875 0.0074 -0.0213 -0.0220 91 LYS A CG 724 C CD . LYS A 92 ? 0.5778 0.5287 0.5705 0.0081 -0.0169 -0.0239 91 LYS A CD 725 C CE . LYS A 92 ? 0.7126 0.6762 0.7118 0.0046 -0.0138 -0.0258 91 LYS A CE 726 N NZ . LYS A 92 ? 0.8832 0.8506 0.8823 0.0053 -0.0097 -0.0274 91 LYS A NZ 727 N N . ALA A 93 ? 0.5054 0.4324 0.4898 0.0104 -0.0307 -0.0167 92 ALA A N 728 C CA . ALA A 93 ? 0.4851 0.4085 0.4640 0.0126 -0.0307 -0.0135 92 ALA A CA 729 C C . ALA A 93 ? 0.5719 0.4937 0.5465 0.0139 -0.0306 -0.0124 92 ALA A C 730 O O . ALA A 93 ? 0.6233 0.5439 0.5966 0.0130 -0.0335 -0.0116 92 ALA A O 731 C CB . ALA A 93 ? 0.4093 0.3305 0.3864 0.0121 -0.0345 -0.0109 92 ALA A CB 732 N N . VAL A 94 ? 0.4273 0.3492 0.4000 0.0156 -0.0272 -0.0121 93 VAL A N 733 C CA . VAL A 94 ? 0.4467 0.3671 0.4151 0.0168 -0.0269 -0.0107 93 VAL A CA 734 C C . VAL A 94 ? 0.5191 0.4374 0.4835 0.0173 -0.0283 -0.0079 93 VAL A C 735 O O . VAL A 94 ? 0.4898 0.4085 0.4549 0.0176 -0.0270 -0.0077 93 VAL A O 736 C CB . VAL A 94 ? 0.5092 0.4318 0.4785 0.0180 -0.0224 -0.0121 93 VAL A CB 737 C CG1 . VAL A 94 ? 0.4759 0.3971 0.4407 0.0192 -0.0221 -0.0104 93 VAL A CG1 738 C CG2 . VAL A 94 ? 0.4905 0.4164 0.4641 0.0172 -0.0204 -0.0158 93 VAL A CG2 739 N N . THR A 95 ? 0.5689 0.4854 0.5297 0.0172 -0.0308 -0.0060 94 THR A N 740 C CA . THR A 95 ? 0.6004 0.5154 0.5577 0.0172 -0.0321 -0.0041 94 THR A CA 741 C C . THR A 95 ? 0.4946 0.4091 0.4484 0.0181 -0.0308 -0.0030 94 THR A C 742 O O . THR A 95 ? 0.4405 0.3554 0.3938 0.0187 -0.0298 -0.0031 94 THR A O 743 C CB . THR A 95 ? 0.6129 0.5269 0.5697 0.0157 -0.0361 -0.0029 94 THR A CB 744 O OG1 . THR A 95 ? 0.5653 0.4790 0.5215 0.0151 -0.0380 -0.0022 94 THR A OG1 745 C CG2 . THR A 95 ? 0.5520 0.4667 0.5126 0.0148 -0.0374 -0.0039 94 THR A CG2 746 N N . PHE A 96 ? 0.4614 0.3753 0.4131 0.0182 -0.0307 -0.0020 95 PHE A N 747 C CA . PHE A 96 ? 0.4575 0.3710 0.4062 0.0187 -0.0297 -0.0010 95 PHE A CA 748 C C . PHE A 96 ? 0.5739 0.4862 0.5203 0.0178 -0.0321 0.0003 95 PHE A C 749 O O . PHE A 96 ? 0.5819 0.4924 0.5269 0.0174 -0.0339 0.0001 95 PHE A O 750 C CB . PHE A 96 ? 0.4594 0.3716 0.4058 0.0198 -0.0282 -0.0016 95 PHE A CB 751 C CG . PHE A 96 ? 0.5491 0.4593 0.4907 0.0206 -0.0280 -0.0011 95 PHE A CG 752 C CD1 . PHE A 96 ? 0.3927 0.3046 0.3350 0.0213 -0.0255 -0.0010 95 PHE A CD1 753 C CD2 . PHE A 96 ? 0.4930 0.3996 0.4296 0.0206 -0.0301 -0.0008 95 PHE A CD2 754 C CE1 . PHE A 96 ? 0.4111 0.3212 0.3491 0.0220 -0.0251 -0.0005 95 PHE A CE1 755 C CE2 . PHE A 96 ? 0.3969 0.3016 0.3293 0.0213 -0.0297 -0.0004 95 PHE A CE2 756 C CZ . PHE A 96 ? 0.4123 0.3188 0.3454 0.0220 -0.0272 -0.0003 95 PHE A CZ 757 N N . PRO A 97 ? 0.6161 0.5282 0.5608 0.0176 -0.0326 0.0013 96 PRO A N 758 C CA . PRO A 97 ? 0.5338 0.4466 0.4781 0.0184 -0.0311 0.0015 96 PRO A CA 759 C C . PRO A 97 ? 0.5438 0.4569 0.4891 0.0180 -0.0328 0.0016 96 PRO A C 760 O O . PRO A 97 ? 0.6092 0.5229 0.5543 0.0188 -0.0314 0.0014 96 PRO A O 761 C CB . PRO A 97 ? 0.5086 0.4212 0.4506 0.0183 -0.0308 0.0028 96 PRO A CB 762 C CG . PRO A 97 ? 0.4934 0.4053 0.4351 0.0170 -0.0333 0.0036 96 PRO A CG 763 C CD . PRO A 97 ? 0.5760 0.4874 0.5192 0.0167 -0.0343 0.0025 96 PRO A CD 764 N N . LEU A 98 ? 0.3966 0.3096 0.3432 0.0166 -0.0357 0.0019 97 LEU A N 765 C CA . LEU A 98 ? 0.4906 0.4046 0.4382 0.0158 -0.0377 0.0027 97 LEU A CA 766 C C . LEU A 98 ? 0.6221 0.5363 0.5723 0.0164 -0.0371 0.0010 97 LEU A C 767 O O . LEU A 98 ? 0.6973 0.6142 0.6490 0.0156 -0.0381 0.0015 97 LEU A O 768 C CB . LEU A 98 ? 0.6303 0.5448 0.5791 0.0138 -0.0412 0.0037 97 LEU A CB 769 C CG . LEU A 98 ? 0.6841 0.5985 0.6310 0.0132 -0.0415 0.0051 97 LEU A CG 770 C CD1 . LEU A 98 ? 0.6659 0.5810 0.6144 0.0112 -0.0447 0.0059 97 LEU A CD1 771 C CD2 . LEU A 98 ? 0.5739 0.4896 0.5190 0.0136 -0.0400 0.0066 97 LEU A CD2 772 N N . GLY A 99 ? 0.5796 0.4936 0.5315 0.0172 -0.0349 -0.0012 98 GLY A N 773 C CA . GLY A 99 ? 0.5828 0.4976 0.5379 0.0176 -0.0332 -0.0038 98 GLY A CA 774 C C . GLY A 99 ? 0.6734 0.5889 0.6331 0.0161 -0.0347 -0.0057 98 GLY A C 775 O O . GLY A 99 ? 0.6961 0.6113 0.6563 0.0154 -0.0363 -0.0049 98 GLY A O 776 N N . ASN A 100 ? 0.6396 0.5657 0.6055 0.0136 -0.0317 -0.0080 99 ASN A N 777 C CA . ASN A 100 ? 0.6844 0.6150 0.6561 0.0116 -0.0311 -0.0104 99 ASN A CA 778 C C . ASN A 100 ? 0.7843 0.7207 0.7596 0.0083 -0.0337 -0.0094 99 ASN A C 779 O O . ASN A 100 ? 0.7548 0.6957 0.7297 0.0067 -0.0348 -0.0075 99 ASN A O 780 C CB . ASN A 100 ? 0.6439 0.5832 0.6208 0.0104 -0.0263 -0.0136 99 ASN A CB 781 C CG . ASN A 100 ? 0.7730 0.7231 0.7529 0.0076 -0.0249 -0.0134 99 ASN A CG 782 O OD1 . ASN A 100 ? 0.9338 0.8836 0.9104 0.0076 -0.0265 -0.0108 99 ASN A OD1 783 N ND2 . ASN A 100 ? 0.7214 0.6811 0.7074 0.0051 -0.0218 -0.0160 99 ASN A ND2 784 N N . ALA A 101 ? 0.6958 0.6318 0.6744 0.0073 -0.0347 -0.0106 100 ALA A N 785 C CA . ALA A 101 ? 0.6585 0.6007 0.6416 0.0040 -0.0366 -0.0103 100 ALA A CA 786 C C . ALA A 101 ? 0.6429 0.5895 0.6321 0.0026 -0.0343 -0.0134 100 ALA A C 787 O O . ALA A 101 ? 0.5302 0.4718 0.5188 0.0047 -0.0327 -0.0151 100 ALA A O 788 C CB . ALA A 101 ? 0.6610 0.5957 0.6408 0.0046 -0.0415 -0.0076 100 ALA A CB 789 N N . GLN A 102 ? 0.7122 0.6680 0.7072 -0.0009 -0.0341 -0.0141 101 GLN A N 790 C CA . GLN A 102 ? 0.6142 0.5754 0.6154 -0.0025 -0.0313 -0.0172 101 GLN A CA 791 C C . GLN A 102 ? 0.6372 0.6050 0.6437 -0.0061 -0.0328 -0.0171 101 GLN A C 792 O O . GLN A 102 ? 0.6681 0.6386 0.6743 -0.0076 -0.0353 -0.0150 101 GLN A O 793 C CB . GLN A 102 ? 0.5656 0.5346 0.5696 -0.0032 -0.0265 -0.0196 101 GLN A CB 794 C CG . GLN A 102 ? 0.4334 0.4130 0.4403 -0.0063 -0.0255 -0.0193 101 GLN A CG 795 C CD . GLN A 102 ? 0.5731 0.5598 0.5826 -0.0069 -0.0206 -0.0217 101 GLN A CD 796 O OE1 . GLN A 102 ? 0.6968 0.6793 0.7029 -0.0042 -0.0188 -0.0222 101 GLN A OE1 797 N NE2 . GLN A 102 ? 0.5649 0.5622 0.5804 -0.0103 -0.0185 -0.0234 101 GLN A NE2 798 N N . SER A 103 ? 0.5777 0.5482 0.5893 -0.0072 -0.0310 -0.0195 102 SER A N 799 C CA . SER A 103 ? 0.5884 0.5659 0.6060 -0.0107 -0.0316 -0.0201 102 SER A CA 800 C C . SER A 103 ? 0.6114 0.5939 0.6346 -0.0118 -0.0275 -0.0234 102 SER A C 801 O O . SER A 103 ? 0.5750 0.5528 0.5971 -0.0095 -0.0255 -0.0250 102 SER A O 802 C CB . SER A 103 ? 0.6809 0.6521 0.6975 -0.0105 -0.0360 -0.0182 102 SER A CB 803 O OG . SER A 103 ? 0.7830 0.7503 0.7948 -0.0099 -0.0398 -0.0151 102 SER A OG 804 N N . SER A 104 ? 0.5248 0.5168 0.5542 -0.0154 -0.0263 -0.0246 103 SER A N 805 C CA . SER A 104 ? 0.4609 0.4592 0.4960 -0.0169 -0.0220 -0.0278 103 SER A CA 806 C C . SER A 104 ? 0.5395 0.5374 0.5790 -0.0183 -0.0229 -0.0285 103 SER A C 807 O O . SER A 104 ? 0.5498 0.5465 0.5896 -0.0194 -0.0265 -0.0267 103 SER A O 808 C CB . SER A 104 ? 0.4719 0.4818 0.5110 -0.0201 -0.0193 -0.0289 103 SER A CB 809 O OG . SER A 104 ? 0.5835 0.5982 0.6254 -0.0230 -0.0217 -0.0276 103 SER A OG 810 N N . THR A 105 ? 0.4801 0.4790 0.5230 -0.0181 -0.0194 -0.0313 104 THR A N 811 C CA . THR A 105 ? 0.4805 0.4809 0.5287 -0.0197 -0.0189 -0.0325 104 THR A CA 812 C C . THR A 105 ? 0.5007 0.5103 0.5545 -0.0218 -0.0138 -0.0355 104 THR A C 813 O O . THR A 105 ? 0.4736 0.4836 0.5266 -0.0205 -0.0104 -0.0375 104 THR A O 814 C CB . THR A 105 ? 0.4884 0.4790 0.5345 -0.0168 -0.0199 -0.0327 104 THR A CB 815 O OG1 . THR A 105 ? 0.5427 0.5250 0.5839 -0.0152 -0.0249 -0.0297 104 THR A OG1 816 C CG2 . THR A 105 ? 0.5174 0.5109 0.5685 -0.0181 -0.0179 -0.0337 104 THR A CG2 817 N N . THR A 106 ? 0.4947 0.5106 0.5513 -0.0240 -0.0125 -0.0344 105 THR A N 818 C CA . THR A 106 ? 0.4627 0.4859 0.5223 -0.0249 -0.0074 -0.0358 105 THR A CA 819 C C . THR A 106 ? 0.4794 0.5008 0.5412 -0.0243 -0.0059 -0.0363 105 THR A C 820 O O . THR A 106 ? 0.4613 0.4795 0.5230 -0.0246 -0.0086 -0.0345 105 THR A O 821 C CB . THR A 106 ? 0.4765 0.5072 0.5363 -0.0272 -0.0069 -0.0338 105 THR A CB 822 O OG1 . THR A 106 ? 0.5348 0.5676 0.5927 -0.0276 -0.0080 -0.0333 105 THR A OG1 823 C CG2 . THR A 106 ? 0.3493 0.3858 0.4110 -0.0276 -0.0022 -0.0349 105 THR A CG2 824 N N . VAL A 107 ? 0.3510 0.3746 0.4148 -0.0235 -0.0015 -0.0387 106 VAL A N 825 C CA . VAL A 107 ? 0.3669 0.3884 0.4328 -0.0224 0.0003 -0.0397 106 VAL A CA 826 C C . VAL A 107 ? 0.4168 0.4451 0.4847 -0.0235 0.0044 -0.0403 106 VAL A C 827 O O . VAL A 107 ? 0.3918 0.4243 0.4593 -0.0235 0.0077 -0.0418 106 VAL A O 828 C CB . VAL A 107 ? 0.3779 0.3941 0.4434 -0.0199 0.0018 -0.0420 106 VAL A CB 829 C CG1 . VAL A 107 ? 0.3645 0.3812 0.4330 -0.0189 0.0052 -0.0433 106 VAL A CG1 830 C CG2 . VAL A 107 ? 0.4270 0.4337 0.4889 -0.0181 -0.0028 -0.0406 106 VAL A CG2 831 N N . THR A 108 ? 0.4409 0.4692 0.5100 -0.0241 0.0040 -0.0390 107 THR A N 832 C CA . THR A 108 ? 0.4146 0.4472 0.4847 -0.0245 0.0075 -0.0396 107 THR A CA 833 C C . THR A 108 ? 0.3777 0.4075 0.4500 -0.0230 0.0097 -0.0414 107 THR A C 834 O O . THR A 108 ? 0.3491 0.3743 0.4224 -0.0222 0.0074 -0.0407 107 THR A O 835 C CB . THR A 108 ? 0.4762 0.5109 0.5460 -0.0263 0.0055 -0.0368 107 THR A CB 836 O OG1 . THR A 108 ? 0.5838 0.6208 0.6517 -0.0277 0.0034 -0.0350 107 THR A OG1 837 C CG2 . THR A 108 ? 0.4016 0.4396 0.4716 -0.0266 0.0088 -0.0374 107 THR A CG2 838 N N . VAL A 109 ? 0.3636 0.3958 0.4361 -0.0223 0.0140 -0.0437 108 VAL A N 839 C CA . VAL A 109 ? 0.2389 0.2689 0.3134 -0.0208 0.0165 -0.0456 108 VAL A CA 840 C C . VAL A 109 ? 0.3779 0.4096 0.4522 -0.0216 0.0176 -0.0450 108 VAL A C 841 O O . VAL A 109 ? 0.3996 0.4344 0.4717 -0.0226 0.0190 -0.0452 108 VAL A O 842 C CB . VAL A 109 ? 0.3211 0.3509 0.3952 -0.0192 0.0203 -0.0490 108 VAL A CB 843 C CG1 . VAL A 109 ? 0.2996 0.3271 0.3755 -0.0176 0.0231 -0.0510 108 VAL A CG1 844 C CG2 . VAL A 109 ? 0.3036 0.3313 0.3782 -0.0181 0.0192 -0.0493 108 VAL A CG2 845 N N . LEU A 110 ? 0.3484 0.3779 0.4248 -0.0213 0.0166 -0.0441 109 LEU A N 846 C CA . LEU A 110 ? 0.2816 0.3122 0.3582 -0.0220 0.0176 -0.0436 109 LEU A CA 847 C C . LEU A 110 ? 0.2952 0.3236 0.3733 -0.0203 0.0207 -0.0461 109 LEU A C 848 O O . LEU A 110 ? 0.4011 0.4268 0.4811 -0.0185 0.0212 -0.0474 109 LEU A O 849 C CB . LEU A 110 ? 0.3784 0.4082 0.4561 -0.0231 0.0141 -0.0405 109 LEU A CB 850 C CG . LEU A 110 ? 0.3278 0.3586 0.4040 -0.0248 0.0103 -0.0378 109 LEU A CG 851 C CD1 . LEU A 110 ? 0.3585 0.3879 0.4354 -0.0258 0.0074 -0.0352 109 LEU A CD1 852 C CD2 . LEU A 110 ? 0.2836 0.3189 0.3577 -0.0261 0.0111 -0.0372 109 LEU A CD2 853 N N . VAL A 111 ? 0.3157 0.3449 0.3928 -0.0206 0.0227 -0.0467 110 VAL A N 854 C CA . VAL A 111 ? 0.2970 0.3235 0.3750 -0.0192 0.0253 -0.0490 110 VAL A CA 855 C C . VAL A 111 ? 0.3639 0.3904 0.4437 -0.0198 0.0248 -0.0477 110 VAL A C 856 O O . VAL A 111 ? 0.3586 0.3877 0.4384 -0.0214 0.0249 -0.0476 110 VAL A O 857 C CB . VAL A 111 ? 0.3298 0.3559 0.4048 -0.0194 0.0282 -0.0522 110 VAL A CB 858 C CG1 . VAL A 111 ? 0.3012 0.3236 0.3762 -0.0184 0.0298 -0.0533 110 VAL A CG1 859 C CG2 . VAL A 111 ? 0.3511 0.3775 0.4237 -0.0192 0.0282 -0.0530 110 VAL A CG2 860 N N . GLU A 112 ? 0.3641 0.3878 0.4464 -0.0184 0.0247 -0.0476 111 GLU A N 861 C CA . GLU A 112 ? 0.4082 0.4317 0.4926 -0.0188 0.0244 -0.0465 111 GLU A CA 862 C C . GLU A 112 ? 0.3589 0.3825 0.4432 -0.0191 0.0279 -0.0498 111 GLU A C 863 O O . GLU A 112 ? 0.3438 0.3650 0.4267 -0.0181 0.0304 -0.0528 111 GLU A O 864 C CB . GLU A 112 ? 0.3601 0.3806 0.4475 -0.0172 0.0237 -0.0459 111 GLU A CB 865 C CG . GLU A 112 ? 0.4710 0.4903 0.5597 -0.0174 0.0198 -0.0435 111 GLU A CG 866 C CD . GLU A 112 ? 0.6177 0.6338 0.7093 -0.0159 0.0189 -0.0428 111 GLU A CD 867 O OE1 . GLU A 112 ? 0.6235 0.6393 0.7171 -0.0144 0.0220 -0.0446 111 GLU A OE1 868 O OE2 . GLU A 112 ? 0.7758 0.7894 0.8674 -0.0162 0.0150 -0.0405 111 GLU A OE2 869 N N . PRO A 113 ? 0.3787 0.4041 0.4639 -0.0206 0.0280 -0.0495 112 PRO A N 870 C CA . PRO A 113 ? 0.3795 0.4043 0.4647 -0.0210 0.0310 -0.0525 112 PRO A CA 871 C C . PRO A 113 ? 0.4238 0.4451 0.5111 -0.0194 0.0322 -0.0533 112 PRO A C 872 O O . PRO A 113 ? 0.4617 0.4821 0.5513 -0.0184 0.0304 -0.0509 112 PRO A O 873 C CB . PRO A 113 ? 0.3997 0.4277 0.4858 -0.0229 0.0302 -0.0512 112 PRO A CB 874 C CG . PRO A 113 ? 0.3186 0.3473 0.4063 -0.0230 0.0265 -0.0472 112 PRO A CG 875 C CD . PRO A 113 ? 0.3472 0.3750 0.4334 -0.0221 0.0250 -0.0463 112 PRO A CD 876 N N . THR A 114 ? 0.3922 0.4115 0.4780 -0.0195 0.0345 -0.0558 113 THR A N 877 C CA . THR A 114 ? 0.4133 0.4303 0.4997 -0.0188 0.0348 -0.0546 113 THR A CA 878 C C . THR A 114 ? 0.4418 0.4595 0.5307 -0.0198 0.0364 -0.0563 113 THR A C 879 O O . THR A 114 ? 0.4011 0.4199 0.4885 -0.0214 0.0377 -0.0582 113 THR A O 880 C CB . THR A 114 ? 0.4367 0.4520 0.5191 -0.0187 0.0350 -0.0539 113 THR A CB 881 O OG1 . THR A 114 ? 0.4395 0.4542 0.5198 -0.0177 0.0335 -0.0523 113 THR A OG1 882 C CG2 . THR A 114 ? 0.4152 0.4281 0.4980 -0.0180 0.0351 -0.0527 113 THR A CG2 883 N N . VAL A 115 ? 0.4271 0.4440 0.5199 -0.0190 0.0361 -0.0555 114 VAL A N 884 C CA . VAL A 115 ? 0.3966 0.4153 0.4913 -0.0203 0.0362 -0.0550 114 VAL A CA 885 C C . VAL A 115 ? 0.4102 0.4258 0.5064 -0.0196 0.0381 -0.0563 114 VAL A C 886 O O . VAL A 115 ? 0.4215 0.4353 0.5179 -0.0181 0.0371 -0.0542 114 VAL A O 887 C CB . VAL A 115 ? 0.4267 0.4476 0.5234 -0.0207 0.0329 -0.0509 114 VAL A CB 888 C CG1 . VAL A 115 ? 0.3943 0.4169 0.4929 -0.0221 0.0328 -0.0501 114 VAL A CG1 889 C CG2 . VAL A 115 ? 0.3880 0.4116 0.4827 -0.0216 0.0306 -0.0493 114 VAL A CG2 890 N N . SER A 116 ? 0.3973 0.4133 0.4934 -0.0209 0.0399 -0.0581 115 SER A N 891 C CA . SER A 116 ? 0.4426 0.4569 0.5395 -0.0207 0.0408 -0.0577 115 SER A CA 892 C C . SER A 116 ? 0.4005 0.4158 0.4999 -0.0220 0.0424 -0.0596 115 SER A C 893 O O . SER A 116 ? 0.3935 0.4118 0.4914 -0.0237 0.0423 -0.0599 115 SER A O 894 C CB . SER A 116 ? 0.3708 0.3837 0.4637 -0.0210 0.0413 -0.0575 115 SER A CB 895 O OG . SER A 116 ? 0.4403 0.4548 0.5310 -0.0226 0.0423 -0.0596 115 SER A OG 896 N N . LEU A 117 ? 0.5058 0.5197 0.6079 -0.0215 0.0429 -0.0590 116 LEU A N 897 C CA . LEU A 117 ? 0.5302 0.5457 0.6339 -0.0228 0.0436 -0.0589 116 LEU A CA 898 C C . LEU A 117 ? 0.5299 0.5425 0.6337 -0.0227 0.0457 -0.0605 116 LEU A C 899 O O . LEU A 117 ? 0.4864 0.4971 0.5903 -0.0214 0.0450 -0.0586 116 LEU A O 900 C CB . LEU A 117 ? 0.5701 0.5875 0.6768 -0.0227 0.0411 -0.0551 116 LEU A CB 901 C CG . LEU A 117 ? 0.4920 0.5114 0.6003 -0.0242 0.0413 -0.0543 116 LEU A CG 902 C CD1 . LEU A 117 ? 0.4834 0.5061 0.5895 -0.0261 0.0414 -0.0550 116 LEU A CD1 903 C CD2 . LEU A 117 ? 0.5432 0.5637 0.6543 -0.0241 0.0384 -0.0504 116 LEU A CD2 904 N N . ILE A 118 ? 0.5477 0.5611 0.6507 -0.0243 0.0475 -0.0626 117 ILE A N 905 C CA . ILE A 118 ? 0.5961 0.6079 0.6986 -0.0246 0.0487 -0.0628 117 ILE A CA 906 C C . ILE A 118 ? 0.6146 0.6270 0.7197 -0.0257 0.0504 -0.0645 117 ILE A C 907 O O . ILE A 118 ? 0.6353 0.6507 0.7408 -0.0269 0.0502 -0.0647 117 ILE A O 908 C CB . ILE A 118 ? 0.6190 0.6306 0.7172 -0.0255 0.0491 -0.0636 117 ILE A CB 909 C CG1 . ILE A 118 ? 0.5988 0.6129 0.6957 -0.0273 0.0501 -0.0661 117 ILE A CG1 910 C CG2 . ILE A 118 ? 0.5337 0.5444 0.6293 -0.0243 0.0475 -0.0618 117 ILE A CG2 911 C CD1 . ILE A 118 ? 0.6271 0.6410 0.7206 -0.0284 0.0507 -0.0671 117 ILE A CD1 912 N N . LYS A 119 ? 0.6447 0.6555 0.7510 -0.0255 0.0514 -0.0641 118 LYS A N 913 C CA . LYS A 119 ? 0.7617 0.7725 0.8710 -0.0263 0.0529 -0.0653 118 LYS A CA 914 C C . LYS A 119 ? 0.7017 0.7136 0.8093 -0.0283 0.0548 -0.0678 118 LYS A C 915 O O . LYS A 119 ? 0.8045 0.8165 0.9143 -0.0291 0.0562 -0.0689 118 LYS A O 916 C CB . LYS A 119 ? 0.6796 0.6882 0.7911 -0.0250 0.0530 -0.0635 118 LYS A CB 917 C CG . LYS A 119 ? 0.9054 0.9134 1.0187 -0.0258 0.0548 -0.0646 118 LYS A CG 918 C CD . LYS A 119 ? 0.8629 0.8728 0.9798 -0.0261 0.0544 -0.0635 118 LYS A CD 919 C CE . LYS A 119 ? 1.0080 1.0163 1.1277 -0.0260 0.0558 -0.0635 118 LYS A CE 920 N NZ . LYS A 119 ? 0.9386 0.9491 1.0615 -0.0257 0.0536 -0.0596 118 LYS A NZ 921 N N . GLY A 120 ? 0.6588 0.6718 0.7627 -0.0292 0.0547 -0.0689 119 GLY A N 922 C CA . GLY A 120 ? 0.7981 0.8124 0.9006 -0.0311 0.0562 -0.0713 119 GLY A CA 923 C C . GLY A 120 ? 0.9898 1.0025 1.0917 -0.0315 0.0574 -0.0716 119 GLY A C 924 O O . GLY A 120 ? 0.9106 0.9212 1.0142 -0.0305 0.0575 -0.0703 119 GLY A O 925 N N . PRO A 121 ? 1.0705 1.0842 1.1701 -0.0331 0.0584 -0.0735 120 PRO A N 926 C CA . PRO A 121 ? 1.0526 1.0647 1.1508 -0.0335 0.0592 -0.0737 120 PRO A CA 927 C C . PRO A 121 ? 1.1957 1.2065 1.2962 -0.0339 0.0609 -0.0743 120 PRO A C 928 O O . PRO A 121 ? 1.1930 1.2017 1.2939 -0.0332 0.0611 -0.0734 120 PRO A O 929 C CB . PRO A 121 ? 0.9703 0.9843 1.0655 -0.0351 0.0595 -0.0756 120 PRO A CB 930 C CG . PRO A 121 ? 1.0155 1.0320 1.1115 -0.0362 0.0599 -0.0771 120 PRO A CG 931 C CD . PRO A 121 ? 0.9853 1.0017 1.0838 -0.0349 0.0590 -0.0757 120 PRO A CD 932 N N . ASP A 122 ? 1.1505 1.1628 1.2527 -0.0350 0.0620 -0.0759 121 ASP A N 933 C CA . ASP A 122 ? 1.1194 1.1308 1.2239 -0.0356 0.0638 -0.0767 121 ASP A CA 934 C C . ASP A 122 ? 1.1529 1.1632 1.2612 -0.0343 0.0637 -0.0753 121 ASP A C 935 O O . ASP A 122 ? 1.2266 1.2375 1.3360 -0.0333 0.0624 -0.0742 121 ASP A O 936 C CB . ASP A 122 ? 1.0422 1.0557 1.1463 -0.0376 0.0652 -0.0793 121 ASP A CB 937 C CG . ASP A 122 ? 1.0868 1.1012 1.1874 -0.0390 0.0656 -0.0808 121 ASP A CG 938 O OD1 . ASP A 122 ? 1.0185 1.0313 1.1178 -0.0385 0.0653 -0.0801 121 ASP A OD1 939 O OD2 . ASP A 122 ? 0.9446 0.9613 1.0440 -0.0406 0.0661 -0.0826 121 ASP A OD2 940 N N . SER A 123 ? 1.1774 1.1861 1.2879 -0.0342 0.0650 -0.0753 122 SER A N 941 C CA . SER A 123 ? 1.2433 1.2508 1.3577 -0.0329 0.0649 -0.0738 122 SER A CA 942 C C . SER A 123 ? 1.2677 1.2767 1.3848 -0.0338 0.0659 -0.0748 122 SER A C 943 O O . SER A 123 ? 1.3277 1.3385 1.4436 -0.0355 0.0669 -0.0764 122 SER A O 944 C CB . SER A 123 ? 1.2590 1.2641 1.3745 -0.0321 0.0656 -0.0727 122 SER A CB 945 O OG . SER A 123 ? 1.2970 1.3008 1.4110 -0.0308 0.0641 -0.0708 122 SER A OG 946 N N . LEU A 124 ? 1.2599 1.2702 1.3798 -0.0327 0.0642 -0.0713 123 LEU A N 947 C CA . LEU A 124 ? 1.3478 1.3622 1.4689 -0.0336 0.0625 -0.0685 123 LEU A CA 948 C C . LEU A 124 ? 1.3678 1.3821 1.4916 -0.0341 0.0637 -0.0682 123 LEU A C 949 O O . LEU A 124 ? 1.2531 1.2660 1.3799 -0.0330 0.0634 -0.0663 123 LEU A O 950 C CB . LEU A 124 ? 1.2911 1.3069 1.4136 -0.0323 0.0595 -0.0648 123 LEU A CB 951 C CG . LEU A 124 ? 1.2269 1.2429 1.3472 -0.0315 0.0580 -0.0646 123 LEU A CG 952 C CD1 . LEU A 124 ? 1.0404 1.0525 1.1616 -0.0296 0.0584 -0.0647 123 LEU A CD1 953 C CD2 . LEU A 124 ? 1.0173 1.0368 1.1378 -0.0317 0.0549 -0.0611 123 LEU A CD2 954 N N . ILE A 125 ? 1.4470 1.4628 1.5698 -0.0359 0.0650 -0.0698 124 ILE A N 955 C CA . ILE A 125 ? 1.3889 1.4045 1.5140 -0.0365 0.0663 -0.0697 124 ILE A CA 956 C C . ILE A 125 ? 1.4342 1.4538 1.5595 -0.0380 0.0652 -0.0680 124 ILE A C 957 O O . ILE A 125 ? 1.4728 1.4950 1.5955 -0.0392 0.0647 -0.0688 124 ILE A O 958 C CB . ILE A 125 ? 1.4297 1.4423 1.5540 -0.0372 0.0695 -0.0735 124 ILE A CB 959 C CG1 . ILE A 125 ? 1.3731 1.3868 1.4937 -0.0388 0.0703 -0.0765 124 ILE A CG1 960 C CG2 . ILE A 125 ? 1.4780 1.4861 1.6032 -0.0357 0.0707 -0.0746 124 ILE A CG2 961 C CD1 . ILE A 125 ? 1.1930 1.2062 1.3132 -0.0404 0.0728 -0.0792 124 ILE A CD1 962 N N . ASP A 126 ? 1.3769 1.3969 1.5053 -0.0380 0.0650 -0.0660 125 ASP A N 963 C CA . ASP A 126 ? 1.3145 1.3378 1.4444 -0.0388 0.0630 -0.0630 125 ASP A CA 964 C C . ASP A 126 ? 1.3107 1.3361 1.4394 -0.0408 0.0641 -0.0644 125 ASP A C 965 O O . ASP A 126 ? 1.2873 1.3114 1.4149 -0.0415 0.0667 -0.0677 125 ASP A O 966 C CB . ASP A 126 ? 1.2972 1.3192 1.4311 -0.0379 0.0627 -0.0606 125 ASP A CB 967 C CG . ASP A 126 ? 1.2900 1.3147 1.4256 -0.0382 0.0596 -0.0567 125 ASP A CG 968 O OD1 . ASP A 126 ? 1.3991 1.4229 1.5378 -0.0374 0.0589 -0.0544 125 ASP A OD1 969 O OD2 . ASP A 126 ? 1.3542 1.3818 1.4880 -0.0393 0.0579 -0.0558 125 ASP A OD2 970 N N . GLY A 127 ? 1.3224 1.3513 1.4513 -0.0418 0.0619 -0.0619 126 GLY A N 971 C CA . GLY A 127 ? 1.2421 1.2735 1.3701 -0.0437 0.0624 -0.0627 126 GLY A CA 972 C C . GLY A 127 ? 1.3792 1.4113 1.5034 -0.0447 0.0638 -0.0660 126 GLY A C 973 O O . GLY A 127 ? 1.3126 1.3468 1.4358 -0.0464 0.0644 -0.0668 126 GLY A O 974 N N . GLY A 128 ? 1.3849 1.4154 1.5070 -0.0440 0.0643 -0.0678 127 GLY A N 975 C CA . GLY A 128 ? 1.4285 1.4589 1.5472 -0.0449 0.0660 -0.0715 127 GLY A CA 976 C C . GLY A 128 ? 1.4062 1.4396 1.5220 -0.0456 0.0643 -0.0711 127 GLY A C 977 O O . GLY A 128 ? 1.3691 1.4052 1.4855 -0.0456 0.0618 -0.0681 127 GLY A O 978 N N . ASN A 129 ? 1.3558 1.3886 1.4685 -0.0461 0.0656 -0.0744 128 ASN A N 979 C CA . ASN A 129 ? 1.2588 1.2942 1.3684 -0.0468 0.0643 -0.0746 128 ASN A CA 980 C C . ASN A 129 ? 1.1947 1.2301 1.3042 -0.0453 0.0621 -0.0724 128 ASN A C 981 O O . ASN A 129 ? 1.0856 1.1185 1.1971 -0.0437 0.0619 -0.0714 128 ASN A O 982 C CB . ASN A 129 ? 1.3254 1.3598 1.4318 -0.0478 0.0664 -0.0788 128 ASN A CB 983 C CG . ASN A 129 ? 1.2575 1.2955 1.3609 -0.0493 0.0658 -0.0795 128 ASN A CG 984 O OD1 . ASN A 129 ? 1.2466 1.2869 1.3490 -0.0491 0.0636 -0.0775 128 ASN A OD1 985 N ND2 . ASN A 129 ? 1.2524 1.2907 1.3544 -0.0510 0.0676 -0.0823 128 ASN A ND2 986 N N . GLU A 130 ? 1.1802 1.2183 1.2875 -0.0457 0.0605 -0.0717 129 GLU A N 987 C CA . GLU A 130 ? 1.0812 1.1194 1.1882 -0.0444 0.0584 -0.0699 129 GLU A CA 988 C C . GLU A 130 ? 0.9859 1.0204 1.0918 -0.0432 0.0597 -0.0721 129 GLU A C 989 O O . GLU A 130 ? 0.8822 0.9153 0.9862 -0.0439 0.0618 -0.0756 129 GLU A O 990 C CB . GLU A 130 ? 0.9612 1.0026 1.0654 -0.0453 0.0569 -0.0695 129 GLU A CB 991 C CG . GLU A 130 ? 1.0136 1.0550 1.1144 -0.0465 0.0590 -0.0735 129 GLU A CG 992 C CD . GLU A 130 ? 1.0559 1.0989 1.1540 -0.0464 0.0577 -0.0736 129 GLU A CD 993 O OE1 . GLU A 130 ? 1.1673 1.2081 1.2635 -0.0460 0.0588 -0.0761 129 GLU A OE1 994 O OE2 . GLU A 130 ? 1.1559 1.2021 1.2538 -0.0469 0.0558 -0.0713 129 GLU A OE2 995 N N . THR A 131 ? 0.9548 0.9878 1.0622 -0.0415 0.0584 -0.0702 130 THR A N 996 C CA . THR A 131 ? 0.8279 0.8573 0.9347 -0.0401 0.0593 -0.0718 130 THR A CA 997 C C . THR A 131 ? 0.9167 0.9467 1.0231 -0.0389 0.0569 -0.0696 130 THR A C 998 O O . THR A 131 ? 0.9769 1.0090 1.0848 -0.0386 0.0546 -0.0662 130 THR A O 999 C CB . THR A 131 ? 0.7416 0.7678 0.8514 -0.0391 0.0605 -0.0718 130 THR A CB 1000 N N . VAL A 132 ? 0.7615 0.7895 0.8657 -0.0382 0.0575 -0.0716 131 VAL A N 1001 C CA . VAL A 132 ? 0.7019 0.7300 0.8054 -0.0370 0.0555 -0.0699 131 VAL A CA 1002 C C . VAL A 132 ? 0.6729 0.6982 0.7792 -0.0351 0.0550 -0.0681 131 VAL A C 1003 O O . VAL A 132 ? 0.6777 0.6994 0.7844 -0.0343 0.0566 -0.0701 131 VAL A O 1004 C CB . VAL A 132 ? 0.7077 0.7345 0.8079 -0.0370 0.0563 -0.0727 131 VAL A CB 1005 C CG1 . VAL A 132 ? 0.6971 0.7239 0.7968 -0.0356 0.0542 -0.0708 131 VAL A CG1 1006 C CG2 . VAL A 132 ? 0.5493 0.5789 0.6468 -0.0389 0.0568 -0.0745 131 VAL A CG2 1007 N N . ALA A 133 ? 0.7203 0.7473 0.8287 -0.0346 0.0526 -0.0645 132 ALA A N 1008 C CA . ALA A 133 ? 0.7795 0.8041 0.8907 -0.0329 0.0520 -0.0626 132 ALA A CA 1009 C C . ALA A 133 ? 0.6806 0.7034 0.7908 -0.0313 0.0510 -0.0624 132 ALA A C 1010 O O . ALA A 133 ? 0.7055 0.7251 0.8172 -0.0298 0.0515 -0.0625 132 ALA A O 1011 C CB . ALA A 133 ? 0.8067 0.8335 0.9206 -0.0331 0.0496 -0.0588 132 ALA A CB 1012 N N . ALA A 134 ? 0.6585 0.6833 0.7663 -0.0316 0.0498 -0.0622 133 ALA A N 1013 C CA . ALA A 134 ? 0.6501 0.6733 0.7569 -0.0302 0.0487 -0.0618 133 ALA A CA 1014 C C . ALA A 134 ? 0.6506 0.6758 0.7540 -0.0310 0.0483 -0.0628 133 ALA A C 1015 O O . ALA A 134 ? 0.6416 0.6702 0.7441 -0.0325 0.0478 -0.0624 133 ALA A O 1016 C CB . ALA A 134 ? 0.7047 0.7285 0.8138 -0.0292 0.0459 -0.0579 133 ALA A CB 1017 N N . VAL A 135 ? 0.6615 0.6845 0.7631 -0.0299 0.0485 -0.0641 134 VAL A N 1018 C CA . VAL A 135 ? 0.6830 0.7075 0.7815 -0.0304 0.0480 -0.0650 134 VAL A CA 1019 C C . VAL A 135 ? 0.6158 0.6399 0.7144 -0.0289 0.0459 -0.0628 134 VAL A C 1020 O O . VAL A 135 ? 0.5876 0.6083 0.6872 -0.0273 0.0462 -0.0629 134 VAL A O 1021 C CB . VAL A 135 ? 0.7081 0.7301 0.8040 -0.0309 0.0503 -0.0691 134 VAL A CB 1022 C CG1 . VAL A 135 ? 0.6028 0.6266 0.6954 -0.0315 0.0497 -0.0699 134 VAL A CG1 1023 C CG2 . VAL A 135 ? 0.7497 0.7718 0.8458 -0.0324 0.0524 -0.0713 134 VAL A CG2 1024 N N . CYS A 136 ? 0.5903 0.6176 0.6880 -0.0294 0.0438 -0.0607 135 CYS A N 1025 C CA . CYS A 136 ? 0.5430 0.5701 0.6404 -0.0282 0.0417 -0.0586 135 CYS A CA 1026 C C . CYS A 136 ? 0.5345 0.5624 0.6285 -0.0285 0.0418 -0.0602 135 CYS A C 1027 O O . CYS A 136 ? 0.4907 0.5214 0.5830 -0.0300 0.0419 -0.0608 135 CYS A O 1028 C CB . CYS A 136 ? 0.5176 0.5474 0.6168 -0.0286 0.0386 -0.0546 135 CYS A CB 1029 S SG . CYS A 136 ? 0.5315 0.5603 0.6314 -0.0271 0.0355 -0.0515 135 CYS A SG 1030 N N . VAL A 137 ? 0.4902 0.5155 0.5833 -0.0271 0.0418 -0.0609 136 VAL A N 1031 C CA . VAL A 137 ? 0.3982 0.4237 0.4881 -0.0272 0.0420 -0.0624 136 VAL A CA 1032 C C . VAL A 137 ? 0.4708 0.4961 0.5608 -0.0258 0.0398 -0.0599 136 VAL A C 1033 O O . VAL A 137 ? 0.4776 0.5002 0.5692 -0.0242 0.0394 -0.0591 136 VAL A O 1034 C CB . VAL A 137 ? 0.5356 0.5575 0.6236 -0.0271 0.0440 -0.0655 136 VAL A CB 1035 C CG1 . VAL A 137 ? 0.4281 0.4511 0.5125 -0.0275 0.0434 -0.0657 136 VAL A CG1 1036 C CG2 . VAL A 137 ? 0.5170 0.5389 0.6051 -0.0284 0.0458 -0.0671 136 VAL A CG2 1037 N N . ALA A 138 ? 0.4461 0.4744 0.5345 -0.0265 0.0383 -0.0587 137 ALA A N 1038 C CA . ALA A 138 ? 0.4659 0.4941 0.5537 -0.0254 0.0363 -0.0568 137 ALA A CA 1039 C C . ALA A 138 ? 0.3911 0.4191 0.4756 -0.0256 0.0373 -0.0591 137 ALA A C 1040 O O . ALA A 138 ? 0.3738 0.4049 0.4564 -0.0269 0.0370 -0.0592 137 ALA A O 1041 C CB . ALA A 138 ? 0.4051 0.4366 0.4939 -0.0263 0.0332 -0.0531 137 ALA A CB 1042 N N . ALA A 139 ? 0.4425 0.4667 0.5261 -0.0244 0.0384 -0.0611 138 ALA A N 1043 C CA . ALA A 139 ? 0.3781 0.4021 0.4581 -0.0250 0.0389 -0.0622 138 ALA A CA 1044 C C . ALA A 139 ? 0.3831 0.4074 0.4616 -0.0242 0.0374 -0.0610 138 ALA A C 1045 O O . ALA A 139 ? 0.3761 0.3989 0.4557 -0.0226 0.0361 -0.0591 138 ALA A O 1046 C CB . ALA A 139 ? 0.3575 0.3789 0.4363 -0.0245 0.0391 -0.0612 138 ALA A CB 1047 N N . THR A 140 ? 0.4967 0.5229 0.5725 -0.0253 0.0375 -0.0621 139 THR A N 1048 C CA . THR A 140 ? 0.3926 0.4190 0.4661 -0.0248 0.0363 -0.0611 139 THR A CA 1049 C C . THR A 140 ? 0.3728 0.3993 0.4482 -0.0235 0.0350 -0.0599 139 THR A C 1050 O O . THR A 140 ? 0.3728 0.3975 0.4479 -0.0220 0.0338 -0.0579 139 THR A O 1051 C CB . THR A 140 ? 0.3498 0.3736 0.4211 -0.0240 0.0359 -0.0596 139 THR A CB 1052 O OG1 . THR A 140 ? 0.3894 0.4105 0.4622 -0.0230 0.0358 -0.0583 139 THR A OG1 1053 C CG2 . THR A 140 ? 0.4019 0.4266 0.4712 -0.0256 0.0368 -0.0611 139 THR A CG2 1054 N N . GLY A 141 ? 0.4025 0.4326 0.4792 -0.0243 0.0336 -0.0576 140 GLY A N 1055 C CA . GLY A 141 ? 0.3614 0.3929 0.4393 -0.0238 0.0308 -0.0539 140 GLY A CA 1056 C C . GLY A 141 ? 0.3474 0.3823 0.4232 -0.0249 0.0296 -0.0529 140 GLY A C 1057 O O . GLY A 141 ? 0.3621 0.3992 0.4363 -0.0263 0.0308 -0.0545 140 GLY A O 1058 N N . LYS A 142 ? 0.3595 0.3945 0.4353 -0.0243 0.0272 -0.0503 141 LYS A N 1059 C CA . LYS A 142 ? 0.3473 0.3853 0.4212 -0.0253 0.0259 -0.0492 141 LYS A CA 1060 C C . LYS A 142 ? 0.3484 0.3873 0.4237 -0.0259 0.0223 -0.0454 141 LYS A C 1061 O O . LYS A 142 ? 0.3328 0.3692 0.4089 -0.0249 0.0203 -0.0436 141 LYS A O 1062 C CB . LYS A 142 ? 0.3707 0.4074 0.4424 -0.0243 0.0265 -0.0505 141 LYS A CB 1063 C CG . LYS A 142 ? 0.3250 0.3648 0.3945 -0.0252 0.0255 -0.0495 141 LYS A CG 1064 C CD . LYS A 142 ? 0.3521 0.3905 0.4196 -0.0241 0.0259 -0.0505 141 LYS A CD 1065 C CE . LYS A 142 ? 0.3424 0.3838 0.4083 -0.0249 0.0244 -0.0488 141 LYS A CE 1066 N NZ . LYS A 142 ? 0.3902 0.4321 0.4574 -0.0252 0.0209 -0.0451 141 LYS A NZ 1067 N N . PRO A 143 ? 0.3410 0.3830 0.4164 -0.0276 0.0212 -0.0440 142 PRO A N 1068 C CA . PRO A 143 ? 0.3337 0.3785 0.4082 -0.0289 0.0234 -0.0461 142 PRO A CA 1069 C C . PRO A 143 ? 0.3937 0.4375 0.4700 -0.0290 0.0251 -0.0475 142 PRO A C 1070 O O . PRO A 143 ? 0.4012 0.4420 0.4791 -0.0278 0.0252 -0.0474 142 PRO A O 1071 C CB . PRO A 143 ? 0.2412 0.2891 0.3156 -0.0305 0.0210 -0.0435 142 PRO A CB 1072 C CG . PRO A 143 ? 0.4110 0.4572 0.4873 -0.0304 0.0176 -0.0403 142 PRO A CG 1073 C CD . PRO A 143 ? 0.3871 0.4298 0.4633 -0.0286 0.0174 -0.0404 142 PRO A CD 1074 N N . VAL A 144 ? 0.3440 0.3902 0.4200 -0.0304 0.0264 -0.0487 143 VAL A N 1075 C CA . VAL A 144 ? 0.3918 0.4369 0.4694 -0.0305 0.0282 -0.0502 143 VAL A CA 1076 C C . VAL A 144 ? 0.3283 0.3731 0.4089 -0.0307 0.0259 -0.0471 143 VAL A C 1077 O O . VAL A 144 ? 0.3421 0.3885 0.4231 -0.0316 0.0231 -0.0443 143 VAL A O 1078 C CB . VAL A 144 ? 0.2767 0.3243 0.3529 -0.0321 0.0301 -0.0524 143 VAL A CB 1079 C CG1 . VAL A 144 ? 0.2573 0.3085 0.3338 -0.0336 0.0282 -0.0501 143 VAL A CG1 1080 C CG2 . VAL A 144 ? 0.3058 0.3520 0.3834 -0.0322 0.0322 -0.0544 143 VAL A CG2 1081 N N . ALA A 145 ? 0.3030 0.3451 0.3855 -0.0298 0.0268 -0.0477 144 ALA A N 1082 C CA . ALA A 145 ? 0.4556 0.4973 0.5408 -0.0301 0.0247 -0.0451 144 ALA A CA 1083 C C . ALA A 145 ? 0.3964 0.4407 0.4823 -0.0319 0.0247 -0.0447 144 ALA A C 1084 O O . ALA A 145 ? 0.3590 0.4054 0.4435 -0.0328 0.0267 -0.0468 144 ALA A O 1085 C CB . ALA A 145 ? 0.4106 0.4488 0.4977 -0.0287 0.0258 -0.0459 144 ALA A CB 1086 N N . GLN A 146 ? 0.3953 0.4396 0.4834 -0.0325 0.0223 -0.0419 145 GLN A N 1087 C CA . GLN A 146 ? 0.4394 0.4854 0.5289 -0.0339 0.0225 -0.0415 145 GLN A CA 1088 C C . GLN A 146 ? 0.3827 0.4263 0.4747 -0.0332 0.0233 -0.0417 145 GLN A C 1089 O O . GLN A 146 ? 0.3640 0.4050 0.4571 -0.0321 0.0220 -0.0405 145 GLN A O 1090 C CB . GLN A 146 ? 0.3569 0.4047 0.4467 -0.0353 0.0190 -0.0382 145 GLN A CB 1091 C CG . GLN A 146 ? 0.3769 0.4267 0.4644 -0.0358 0.0180 -0.0376 145 GLN A CG 1092 C CD . GLN A 146 ? 0.6640 0.7149 0.7517 -0.0370 0.0142 -0.0342 145 GLN A CD 1093 O OE1 . GLN A 146 ? 0.7968 0.8500 0.8830 -0.0378 0.0135 -0.0337 145 GLN A OE1 1094 N NE2 . GLN A 146 ? 0.5439 0.5930 0.6333 -0.0373 0.0118 -0.0319 145 GLN A NE2 1095 N N . ILE A 147 ? 0.4299 0.4744 0.5226 -0.0339 0.0255 -0.0434 146 ILE A N 1096 C CA . ILE A 147 ? 0.4740 0.5165 0.5692 -0.0334 0.0265 -0.0437 146 ILE A CA 1097 C C . ILE A 147 ? 0.5376 0.5819 0.6345 -0.0349 0.0253 -0.0419 146 ILE A C 1098 O O . ILE A 147 ? 0.5333 0.5802 0.6294 -0.0362 0.0263 -0.0428 146 ILE A O 1099 C CB . ILE A 147 ? 0.5225 0.5637 0.6171 -0.0328 0.0303 -0.0475 146 ILE A CB 1100 C CG1 . ILE A 147 ? 0.3920 0.4309 0.4851 -0.0312 0.0314 -0.0492 146 ILE A CG1 1101 C CG2 . ILE A 147 ? 0.4217 0.4612 0.5190 -0.0325 0.0313 -0.0475 146 ILE A CG2 1102 C CD1 . ILE A 147 ? 0.4579 0.4953 0.5499 -0.0308 0.0349 -0.0532 146 ILE A CD1 1103 N N . ASP A 148 ? 0.5740 0.6168 0.6731 -0.0348 0.0233 -0.0395 147 ASP A N 1104 C CA . ASP A 148 ? 0.5033 0.5470 0.6043 -0.0361 0.0221 -0.0377 147 ASP A CA 1105 C C . ASP A 148 ? 0.5379 0.5793 0.6414 -0.0352 0.0233 -0.0381 147 ASP A C 1106 O O . ASP A 148 ? 0.4938 0.5325 0.5978 -0.0336 0.0241 -0.0389 147 ASP A O 1107 C CB . ASP A 148 ? 0.6049 0.6489 0.7059 -0.0369 0.0178 -0.0340 147 ASP A CB 1108 C CG . ASP A 148 ? 0.6892 0.7353 0.7911 -0.0387 0.0165 -0.0324 147 ASP A CG 1109 O OD1 . ASP A 148 ? 0.7125 0.7595 0.8156 -0.0391 0.0188 -0.0337 147 ASP A OD1 1110 O OD2 . ASP A 148 ? 0.7595 0.8063 0.8608 -0.0396 0.0133 -0.0298 147 ASP A OD2 1111 N N . TRP A 149 ? 0.5782 0.6204 0.6834 -0.0362 0.0235 -0.0375 148 TRP A N 1112 C CA . TRP A 149 ? 0.6299 0.6701 0.7377 -0.0355 0.0246 -0.0378 148 TRP A CA 1113 C C . TRP A 149 ? 0.5813 0.6212 0.6911 -0.0364 0.0217 -0.0346 148 TRP A C 1114 O O . TRP A 149 ? 0.6701 0.7122 0.7796 -0.0379 0.0199 -0.0330 148 TRP A O 1115 C CB . TRP A 149 ? 0.6168 0.6577 0.7248 -0.0359 0.0282 -0.0407 148 TRP A CB 1116 C CG . TRP A 149 ? 0.6212 0.6614 0.7271 -0.0350 0.0312 -0.0442 148 TRP A CG 1117 C CD1 . TRP A 149 ? 0.6075 0.6497 0.7107 -0.0357 0.0320 -0.0458 148 TRP A CD1 1118 C CD2 . TRP A 149 ? 0.6765 0.7138 0.7828 -0.0335 0.0337 -0.0465 148 TRP A CD2 1119 N NE1 . TRP A 149 ? 0.6527 0.6933 0.7544 -0.0347 0.0348 -0.0491 148 TRP A NE1 1120 C CE2 . TRP A 149 ? 0.6092 0.6466 0.7127 -0.0334 0.0359 -0.0496 148 TRP A CE2 1121 C CE3 . TRP A 149 ? 0.6726 0.7071 0.7813 -0.0323 0.0342 -0.0464 148 TRP A CE3 1122 C CZ2 . TRP A 149 ? 0.5653 0.5999 0.6682 -0.0322 0.0384 -0.0525 148 TRP A CZ2 1123 C CZ3 . TRP A 149 ? 0.6790 0.7108 0.7872 -0.0309 0.0369 -0.0492 148 TRP A CZ3 1124 C CH2 . TRP A 149 ? 0.6683 0.7000 0.7736 -0.0309 0.0389 -0.0523 148 TRP A CH2 1125 N N . GLU A 150 ? 0.5290 0.5662 0.6407 -0.0353 0.0213 -0.0339 149 GLU A N 1126 C CA . GLU A 150 ? 0.6548 0.6913 0.7684 -0.0359 0.0188 -0.0312 149 GLU A CA 1127 C C . GLU A 150 ? 0.7500 0.7855 0.8663 -0.0354 0.0211 -0.0321 149 GLU A C 1128 O O . GLU A 150 ? 0.7094 0.7433 0.8263 -0.0340 0.0239 -0.0343 149 GLU A O 1129 C CB . GLU A 150 ? 0.4567 0.4906 0.5701 -0.0352 0.0157 -0.0290 149 GLU A CB 1130 C CG . GLU A 150 ? 0.4713 0.5062 0.5822 -0.0359 0.0129 -0.0276 149 GLU A CG 1131 C CD . GLU A 150 ? 0.5390 0.5708 0.6492 -0.0351 0.0098 -0.0258 149 GLU A CD 1132 O OE1 . GLU A 150 ? 0.5422 0.5714 0.6539 -0.0337 0.0104 -0.0260 149 GLU A OE1 1133 O OE2 . GLU A 150 ? 0.5872 0.6192 0.6953 -0.0360 0.0069 -0.0241 149 GLU A OE2 1134 N N . GLY A 151 ? 0.9217 0.9579 1.0396 -0.0366 0.0199 -0.0304 150 GLY A N 1135 C CA . GLY A 151 ? 0.8167 0.8527 0.9370 -0.0366 0.0223 -0.0314 150 GLY A CA 1136 C C . GLY A 151 ? 0.8361 0.8749 0.9555 -0.0380 0.0241 -0.0328 150 GLY A C 1137 O O . GLY A 151 ? 0.9044 0.9440 1.0220 -0.0378 0.0263 -0.0353 150 GLY A O 1138 N N . ASP A 152 ? 0.7400 0.7802 0.8605 -0.0394 0.0231 -0.0313 151 ASP A N 1139 C CA . ASP A 152 ? 0.7946 0.8377 0.9142 -0.0409 0.0242 -0.0323 151 ASP A CA 1140 C C . ASP A 152 ? 0.8955 0.9385 1.0166 -0.0409 0.0276 -0.0345 151 ASP A C 1141 O O . ASP A 152 ? 0.8419 0.8852 0.9648 -0.0417 0.0274 -0.0335 151 ASP A O 1142 C CB . ASP A 152 ? 0.9252 0.9700 1.0450 -0.0425 0.0210 -0.0293 151 ASP A CB 1143 C CG . ASP A 152 ? 0.9143 0.9594 1.0320 -0.0428 0.0177 -0.0275 151 ASP A CG 1144 O OD1 . ASP A 152 ? 0.9345 0.9794 1.0504 -0.0420 0.0182 -0.0287 151 ASP A OD1 1145 O OD2 . ASP A 152 ? 1.1167 1.1621 1.2344 -0.0439 0.0147 -0.0248 151 ASP A OD2 1146 N N . LEU A 153 ? 0.8960 0.9381 1.0162 -0.0400 0.0307 -0.0376 152 LEU A N 1147 C CA . LEU A 153 ? 0.7412 0.7826 0.8623 -0.0399 0.0341 -0.0401 152 LEU A CA 1148 C C . LEU A 153 ? 0.7802 0.8231 0.8989 -0.0406 0.0367 -0.0433 152 LEU A C 1149 O O . LEU A 153 ? 0.8452 0.8873 0.9643 -0.0406 0.0396 -0.0457 152 LEU A O 1150 C CB . LEU A 153 ? 0.7619 0.8000 0.8844 -0.0381 0.0357 -0.0412 152 LEU A CB 1151 C CG . LEU A 153 ? 0.9211 0.9574 1.0455 -0.0371 0.0330 -0.0384 152 LEU A CG 1152 C CD1 . LEU A 153 ? 0.8200 0.8532 0.9457 -0.0352 0.0349 -0.0397 152 LEU A CD1 1153 C CD2 . LEU A 153 ? 0.9967 1.0336 1.1234 -0.0381 0.0310 -0.0355 152 LEU A CD2 1154 N N . GLY A 154 ? 0.8423 0.8872 0.9585 -0.0411 0.0358 -0.0434 153 GLY A N 1155 C CA . GLY A 154 ? 0.8209 0.8672 0.9346 -0.0419 0.0381 -0.0465 153 GLY A CA 1156 C C . GLY A 154 ? 0.8506 0.8988 0.9616 -0.0422 0.0367 -0.0462 153 GLY A C 1157 O O . GLY A 154 ? 0.8279 0.8770 0.9391 -0.0423 0.0337 -0.0433 153 GLY A O 1158 N N . GLU A 155 ? 0.8210 0.8699 0.9293 -0.0426 0.0389 -0.0492 154 GLU A N 1159 C CA . GLU A 155 ? 0.7926 0.8436 0.8982 -0.0430 0.0380 -0.0494 154 GLU A CA 1160 C C . GLU A 155 ? 0.8104 0.8596 0.9139 -0.0417 0.0395 -0.0518 154 GLU A C 1161 O O . GLU A 155 ? 0.8061 0.8526 0.9100 -0.0408 0.0416 -0.0540 154 GLU A O 1162 C CB . GLU A 155 ? 0.8212 0.8750 0.9253 -0.0447 0.0391 -0.0509 154 GLU A CB 1163 C CG . GLU A 155 ? 0.9030 0.9594 1.0045 -0.0454 0.0378 -0.0504 154 GLU A CG 1164 C CD . GLU A 155 ? 1.0382 1.0968 1.1377 -0.0469 0.0396 -0.0527 154 GLU A CD 1165 O OE1 . GLU A 155 ? 0.9437 1.0033 1.0403 -0.0471 0.0404 -0.0547 154 GLU A OE1 1166 O OE2 . GLU A 155 ? 1.2448 1.3042 1.3457 -0.0479 0.0401 -0.0526 154 GLU A OE2 1167 N N . MET A 156 ? 0.8584 0.9088 0.9597 -0.0417 0.0382 -0.0515 155 MET A N 1168 C CA . MET A 156 ? 0.8591 0.9079 0.9583 -0.0406 0.0395 -0.0537 155 MET A CA 1169 C C . MET A 156 ? 0.8669 0.9176 0.9627 -0.0415 0.0407 -0.0562 155 MET A C 1170 O O . MET A 156 ? 0.8639 0.9176 0.9590 -0.0429 0.0400 -0.0555 155 MET A O 1171 C CB . MET A 156 ? 0.8063 0.8543 0.9057 -0.0394 0.0370 -0.0513 155 MET A CB 1172 C CG . MET A 156 ? 0.8476 0.8983 0.9463 -0.0402 0.0341 -0.0486 155 MET A CG 1173 S SD . MET A 156 ? 1.0615 1.1120 1.1574 -0.0392 0.0333 -0.0489 155 MET A SD 1174 C CE . MET A 156 ? 0.6570 0.7089 0.7496 -0.0401 0.0362 -0.0529 155 MET A CE 1175 N N . GLU A 157 ? 0.9350 0.9839 1.0289 -0.0408 0.0426 -0.0591 156 GLU A N 1176 C CA . GLU A 157 ? 0.8842 0.9344 0.9747 -0.0416 0.0437 -0.0616 156 GLU A CA 1177 C C . GLU A 157 ? 0.7980 0.8463 0.8869 -0.0402 0.0435 -0.0624 156 GLU A C 1178 O O . GLU A 157 ? 0.7810 0.8260 0.8709 -0.0389 0.0444 -0.0632 156 GLU A O 1179 C CB . GLU A 157 ? 0.8667 0.9162 0.9561 -0.0426 0.0465 -0.0653 156 GLU A CB 1180 C CG . GLU A 157 ? 1.0178 1.0706 1.1061 -0.0445 0.0468 -0.0658 156 GLU A CG 1181 C CD . GLU A 157 ? 1.0090 1.0609 1.0959 -0.0455 0.0496 -0.0697 156 GLU A CD 1182 O OE1 . GLU A 157 ? 1.0322 1.0816 1.1177 -0.0450 0.0510 -0.0723 156 GLU A OE1 1183 O OE2 . GLU A 157 ? 1.0708 1.1243 1.1580 -0.0469 0.0503 -0.0701 156 GLU A OE2 1184 N N . SER A 158 ? 0.7270 0.7772 0.8135 -0.0405 0.0425 -0.0621 157 SER A N 1185 C CA . SER A 158 ? 0.6966 0.7452 0.7817 -0.0392 0.0421 -0.0624 157 SER A CA 1186 C C . SER A 158 ? 0.7767 0.8267 0.8582 -0.0400 0.0428 -0.0647 157 SER A C 1187 O O . SER A 158 ? 0.8541 0.9073 0.9343 -0.0414 0.0426 -0.0647 157 SER A O 1188 C CB . SER A 158 ? 0.7316 0.7807 0.8179 -0.0383 0.0392 -0.0587 157 SER A CB 1189 O OG . SER A 158 ? 0.6627 0.7152 0.7476 -0.0393 0.0376 -0.0573 157 SER A OG 1190 N N . SER A 159 ? 0.7990 0.8467 0.8790 -0.0390 0.0435 -0.0664 158 SER A N 1191 C CA . SER A 159 ? 0.7863 0.8348 0.8629 -0.0395 0.0439 -0.0684 158 SER A CA 1192 C C . SER A 159 ? 0.6926 0.7397 0.7685 -0.0380 0.0427 -0.0674 158 SER A C 1193 O O . SER A 159 ? 0.7044 0.7488 0.7821 -0.0365 0.0423 -0.0663 158 SER A O 1194 C CB . SER A 159 ? 0.6517 0.6984 0.7267 -0.0404 0.0464 -0.0725 158 SER A CB 1195 O OG . SER A 159 ? 0.6105 0.6529 0.6864 -0.0392 0.0473 -0.0738 158 SER A OG 1196 N N . THR A 160 ? 0.7053 0.7542 0.7785 -0.0385 0.0422 -0.0677 159 THR A N 1197 C CA . THR A 160 ? 0.5857 0.6337 0.6580 -0.0372 0.0410 -0.0667 159 THR A CA 1198 C C . THR A 160 ? 0.6122 0.6595 0.6814 -0.0377 0.0421 -0.0698 159 THR A C 1199 O O . THR A 160 ? 0.6010 0.6508 0.6683 -0.0392 0.0427 -0.0713 159 THR A O 1200 C CB . THR A 160 ? 0.6053 0.6566 0.6776 -0.0373 0.0386 -0.0634 159 THR A CB 1201 O OG1 . THR A 160 ? 0.6636 0.7156 0.7389 -0.0372 0.0372 -0.0605 159 THR A OG1 1202 C CG2 . THR A 160 ? 0.5359 0.5860 0.6074 -0.0359 0.0373 -0.0622 159 THR A CG2 1203 N N . THR A 161 ? 0.5945 0.6385 0.6633 -0.0364 0.0423 -0.0706 160 THR A N 1204 C CA . THR A 161 ? 0.6219 0.6647 0.6880 -0.0369 0.0430 -0.0733 160 THR A CA 1205 C C . THR A 161 ? 0.5699 0.6119 0.6352 -0.0355 0.0416 -0.0718 160 THR A C 1206 O O . THR A 161 ? 0.5141 0.5529 0.5807 -0.0340 0.0413 -0.0710 160 THR A O 1207 C CB . THR A 161 ? 0.5934 0.6329 0.6600 -0.0367 0.0441 -0.0742 160 THR A CB 1208 O OG1 . THR A 161 ? 0.7385 0.7748 0.8071 -0.0349 0.0436 -0.0725 160 THR A OG1 1209 C CG2 . THR A 161 ? 0.5892 0.6293 0.6566 -0.0381 0.0456 -0.0760 160 THR A CG2 1210 N N . SER A 162 ? 0.5351 0.5799 0.5981 -0.0361 0.0408 -0.0714 161 SER A N 1211 C CA . SER A 162 ? 0.4538 0.4983 0.5159 -0.0350 0.0394 -0.0700 161 SER A CA 1212 C C . SER A 162 ? 0.4650 0.5069 0.5256 -0.0346 0.0395 -0.0706 161 SER A C 1213 O O . SER A 162 ? 0.4921 0.5337 0.5520 -0.0354 0.0403 -0.0714 161 SER A O 1214 C CB . SER A 162 ? 0.4883 0.5372 0.5488 -0.0357 0.0382 -0.0684 161 SER A CB 1215 O OG . SER A 162 ? 0.7745 0.8261 0.8366 -0.0362 0.0375 -0.0663 161 SER A OG 1216 N N . PHE A 163 ? 0.4814 0.5220 0.5418 -0.0332 0.0383 -0.0689 162 PHE A N 1217 C CA . PHE A 163 ? 0.4956 0.5338 0.5551 -0.0323 0.0378 -0.0676 162 PHE A CA 1218 C C . PHE A 163 ? 0.5197 0.5589 0.5774 -0.0319 0.0366 -0.0668 162 PHE A C 1219 O O . PHE A 163 ? 0.4780 0.5192 0.5355 -0.0320 0.0361 -0.0668 162 PHE A O 1220 C CB . PHE A 163 ? 0.4332 0.4675 0.4944 -0.0305 0.0374 -0.0658 162 PHE A CB 1221 C CG . PHE A 163 ? 0.5253 0.5583 0.5882 -0.0308 0.0385 -0.0664 162 PHE A CG 1222 C CD1 . PHE A 163 ? 0.4721 0.5043 0.5344 -0.0316 0.0393 -0.0672 162 PHE A CD1 1223 C CD2 . PHE A 163 ? 0.4142 0.4468 0.4794 -0.0302 0.0387 -0.0663 162 PHE A CD2 1224 C CE1 . PHE A 163 ? 0.4121 0.4431 0.4760 -0.0318 0.0403 -0.0678 162 PHE A CE1 1225 C CE2 . PHE A 163 ? 0.3483 0.3795 0.4151 -0.0304 0.0397 -0.0668 162 PHE A CE2 1226 C CZ . PHE A 163 ? 0.4551 0.4856 0.5212 -0.0312 0.0405 -0.0675 162 PHE A CZ 1227 N N . PRO A 164 ? 0.6031 0.6411 0.6596 -0.0317 0.0362 -0.0661 163 PRO A N 1228 C CA . PRO A 164 ? 0.6313 0.6707 0.6861 -0.0316 0.0353 -0.0656 163 PRO A CA 1229 C C . PRO A 164 ? 0.5660 0.6040 0.6213 -0.0299 0.0341 -0.0638 163 PRO A C 1230 O O . PRO A 164 ? 0.5701 0.6101 0.6243 -0.0300 0.0334 -0.0636 163 PRO A O 1231 C CB . PRO A 164 ? 0.5659 0.6038 0.6199 -0.0317 0.0353 -0.0653 163 PRO A CB 1232 C CG . PRO A 164 ? 0.5308 0.5678 0.5857 -0.0324 0.0365 -0.0663 163 PRO A CG 1233 C CD . PRO A 164 ? 0.4845 0.5203 0.5413 -0.0317 0.0368 -0.0661 163 PRO A CD 1234 N N . ASN A 165 ? 0.4522 0.4871 0.5093 -0.0284 0.0338 -0.0624 164 ASN A N 1235 C CA . ASN A 165 ? 0.4316 0.4651 0.4894 -0.0268 0.0326 -0.0606 164 ASN A CA 1236 C C . ASN A 165 ? 0.5054 0.5407 0.5646 -0.0268 0.0326 -0.0611 164 ASN A C 1237 O O . ASN A 165 ? 0.5216 0.5559 0.5819 -0.0254 0.0316 -0.0597 164 ASN A O 1238 C CB . ASN A 165 ? 0.3427 0.3723 0.4018 -0.0253 0.0322 -0.0587 164 ASN A CB 1239 C CG . ASN A 165 ? 0.3796 0.4082 0.4405 -0.0253 0.0331 -0.0592 164 ASN A CG 1240 O OD1 . ASN A 165 ? 0.4034 0.4341 0.4651 -0.0263 0.0339 -0.0608 164 ASN A OD1 1241 N ND2 . ASN A 165 ? 0.3575 0.3830 0.4192 -0.0243 0.0328 -0.0578 164 ASN A ND2 1242 N N . GLU A 166 ? 0.5005 0.5385 0.5598 -0.0284 0.0336 -0.0630 165 GLU A N 1243 C CA . GLU A 166 ? 0.4421 0.4835 0.5028 -0.0285 0.0326 -0.0607 165 GLU A CA 1244 C C . GLU A 166 ? 0.4284 0.4682 0.4921 -0.0276 0.0323 -0.0593 165 GLU A C 1245 O O . GLU A 166 ? 0.4408 0.4825 0.5062 -0.0274 0.0305 -0.0563 165 GLU A O 1246 C CB . GLU A 166 ? 0.3971 0.4405 0.4572 -0.0279 0.0306 -0.0578 165 GLU A CB 1247 C CG . GLU A 166 ? 0.3869 0.4329 0.4443 -0.0290 0.0307 -0.0586 165 GLU A CG 1248 C CD . GLU A 166 ? 0.5715 0.6194 0.6285 -0.0284 0.0288 -0.0557 165 GLU A CD 1249 O OE1 . GLU A 166 ? 0.7332 0.7805 0.7883 -0.0281 0.0289 -0.0563 165 GLU A OE1 1250 O OE2 . GLU A 166 ? 0.5091 0.5587 0.5677 -0.0285 0.0271 -0.0528 165 GLU A OE2 1251 N N . THR A 167 ? 0.4425 0.4790 0.5071 -0.0273 0.0337 -0.0615 166 THR A N 1252 C CA . THR A 167 ? 0.3553 0.3906 0.4226 -0.0268 0.0339 -0.0607 166 THR A CA 1253 C C . THR A 167 ? 0.4635 0.5002 0.5308 -0.0284 0.0354 -0.0626 166 THR A C 1254 O O . THR A 167 ? 0.4570 0.4941 0.5222 -0.0297 0.0366 -0.0652 166 THR A O 1255 C CB . THR A 167 ? 0.3547 0.3854 0.4229 -0.0253 0.0343 -0.0611 166 THR A CB 1256 O OG1 . THR A 167 ? 0.3768 0.4064 0.4431 -0.0258 0.0348 -0.0612 166 THR A OG1 1257 C CG2 . THR A 167 ? 0.3902 0.4195 0.4582 -0.0236 0.0327 -0.0590 166 THR A CG2 1258 N N . ALA A 168 ? 0.4438 0.4814 0.5136 -0.0285 0.0351 -0.0612 167 ALA A N 1259 C CA . ALA A 168 ? 0.3832 0.4223 0.4532 -0.0300 0.0365 -0.0627 167 ALA A CA 1260 C C . ALA A 168 ? 0.4299 0.4666 0.5026 -0.0295 0.0372 -0.0628 167 ALA A C 1261 O O . ALA A 168 ? 0.4299 0.4654 0.5048 -0.0282 0.0359 -0.0605 167 ALA A O 1262 C CB . ALA A 168 ? 0.3977 0.4413 0.4678 -0.0313 0.0352 -0.0607 167 ALA A CB 1263 N N . THR A 169 ? 0.4333 0.4691 0.5057 -0.0305 0.0391 -0.0655 168 THR A N 1264 C CA . THR A 169 ? 0.4391 0.4730 0.5141 -0.0302 0.0401 -0.0659 168 THR A CA 1265 C C . THR A 169 ? 0.5203 0.5574 0.5962 -0.0316 0.0401 -0.0652 168 THR A C 1266 O O . THR A 169 ? 0.5385 0.5781 0.6125 -0.0332 0.0407 -0.0665 168 THR A O 1267 C CB . THR A 169 ? 0.3562 0.3868 0.4303 -0.0303 0.0416 -0.0679 168 THR A CB 1268 O OG1 . THR A 169 ? 0.3967 0.4247 0.4703 -0.0286 0.0404 -0.0657 168 THR A OG1 1269 C CG2 . THR A 169 ? 0.4332 0.4625 0.5096 -0.0304 0.0427 -0.0684 168 THR A CG2 1270 N N . ILE A 170 ? 0.5449 0.5820 0.6238 -0.0312 0.0394 -0.0630 169 ILE A N 1271 C CA . ILE A 170 ? 0.5440 0.5836 0.6243 -0.0325 0.0394 -0.0622 169 ILE A CA 1272 C C . ILE A 170 ? 0.5672 0.6041 0.6499 -0.0320 0.0407 -0.0630 169 ILE A C 1273 O O . ILE A 170 ? 0.5504 0.5846 0.6348 -0.0305 0.0402 -0.0619 169 ILE A O 1274 C CB . ILE A 170 ? 0.5140 0.5565 0.5957 -0.0327 0.0366 -0.0582 169 ILE A CB 1275 C CG1 . ILE A 170 ? 0.5541 0.5989 0.6372 -0.0342 0.0366 -0.0575 169 ILE A CG1 1276 C CG2 . ILE A 170 ? 0.4744 0.5149 0.5584 -0.0312 0.0348 -0.0556 169 ILE A CG2 1277 C CD1 . ILE A 170 ? 0.4432 0.4908 0.5274 -0.0349 0.0337 -0.0538 169 ILE A CD1 1278 N N . VAL A 171 ? 0.5599 0.5974 0.6425 -0.0333 0.0425 -0.0650 170 VAL A N 1279 C CA . VAL A 171 ? 0.5358 0.5707 0.6204 -0.0331 0.0440 -0.0661 170 VAL A CA 1280 C C . VAL A 171 ? 0.6554 0.6931 0.7418 -0.0343 0.0436 -0.0646 170 VAL A C 1281 O O . VAL A 171 ? 0.7232 0.7638 0.8082 -0.0359 0.0439 -0.0653 170 VAL A O 1282 C CB . VAL A 171 ? 0.5337 0.5661 0.6167 -0.0337 0.0465 -0.0702 170 VAL A CB 1283 C CG1 . VAL A 171 ? 0.5528 0.5830 0.6381 -0.0337 0.0480 -0.0711 170 VAL A CG1 1284 C CG2 . VAL A 171 ? 0.6066 0.6357 0.6881 -0.0327 0.0466 -0.0715 170 VAL A CG2 1285 N N . SER A 172 ? 0.6250 0.6618 0.7145 -0.0336 0.0428 -0.0624 171 SER A N 1286 C CA . SER A 172 ? 0.6486 0.6877 0.7400 -0.0347 0.0421 -0.0605 171 SER A CA 1287 C C . SER A 172 ? 0.6237 0.6605 0.7173 -0.0345 0.0439 -0.0617 171 SER A C 1288 O O . SER A 172 ? 0.6188 0.6528 0.7143 -0.0330 0.0439 -0.0612 171 SER A O 1289 C CB . SER A 172 ? 0.6648 0.7054 0.7581 -0.0343 0.0390 -0.0564 171 SER A CB 1290 O OG . SER A 172 ? 0.6534 0.6958 0.7487 -0.0355 0.0381 -0.0546 171 SER A OG 1291 N N . GLN A 173 ? 0.7148 0.7528 0.8083 -0.0359 0.0454 -0.0633 172 GLN A N 1292 C CA . GLN A 173 ? 0.8117 0.8479 0.9073 -0.0360 0.0470 -0.0641 172 GLN A CA 1293 C C . GLN A 173 ? 0.7780 0.8166 0.8762 -0.0367 0.0455 -0.0612 172 GLN A C 1294 O O . GLN A 173 ? 0.7042 0.7460 0.8016 -0.0380 0.0445 -0.0601 172 GLN A O 1295 C CB . GLN A 173 ? 0.7508 0.7866 0.8448 -0.0372 0.0497 -0.0679 172 GLN A CB 1296 C CG . GLN A 173 ? 0.7976 0.8305 0.8892 -0.0368 0.0511 -0.0710 172 GLN A CG 1297 C CD . GLN A 173 ? 0.8965 0.9295 0.9861 -0.0385 0.0532 -0.0745 172 GLN A CD 1298 O OE1 . GLN A 173 ? 0.7942 0.8297 0.8839 -0.0399 0.0536 -0.0746 172 GLN A OE1 1299 N NE2 . GLN A 173 ? 0.9410 0.9711 1.0288 -0.0384 0.0545 -0.0775 172 GLN A NE2 1300 N N . TYR A 174 ? 0.7866 0.8233 0.8878 -0.0358 0.0453 -0.0598 173 TYR A N 1301 C CA . TYR A 174 ? 0.6771 0.7154 0.7809 -0.0365 0.0439 -0.0571 173 TYR A CA 1302 C C . TYR A 174 ? 0.7202 0.7577 0.8251 -0.0372 0.0464 -0.0590 173 TYR A C 1303 O O . TYR A 174 ? 0.7180 0.7524 0.8239 -0.0363 0.0482 -0.0606 173 TYR A O 1304 C CB . TYR A 174 ? 0.6696 0.7063 0.7760 -0.0352 0.0419 -0.0540 173 TYR A CB 1305 C CG . TYR A 174 ? 0.7812 0.8200 0.8898 -0.0361 0.0394 -0.0506 173 TYR A CG 1306 C CD1 . TYR A 174 ? 0.7685 0.8100 0.8760 -0.0371 0.0369 -0.0485 173 TYR A CD1 1307 C CD2 . TYR A 174 ? 0.6656 0.7032 0.7772 -0.0360 0.0394 -0.0494 173 TYR A CD2 1308 C CE1 . TYR A 174 ? 0.7889 0.8320 0.8982 -0.0381 0.0344 -0.0454 173 TYR A CE1 1309 C CE2 . TYR A 174 ? 0.7650 0.8043 0.8784 -0.0370 0.0370 -0.0463 173 TYR A CE2 1310 C CZ . TYR A 174 ? 0.8742 0.9161 0.9864 -0.0380 0.0344 -0.0443 173 TYR A CZ 1311 O OH . TYR A 174 ? 0.8260 0.8693 0.9398 -0.0391 0.0318 -0.0412 173 TYR A OH 1312 N N A LYS A 175 ? 0.7928 0.8330 0.8975 -0.0389 0.0465 -0.0589 174 LYS A N 1313 N N B LYS A 175 ? 0.7904 0.8306 0.8950 -0.0389 0.0465 -0.0590 174 LYS A N 1314 C CA A LYS A 175 ? 0.8583 0.8981 0.9638 -0.0398 0.0487 -0.0608 174 LYS A CA 1315 C CA B LYS A 175 ? 0.8602 0.8999 0.9658 -0.0398 0.0487 -0.0608 174 LYS A CA 1316 C C A LYS A 175 ? 0.8832 0.9240 0.9917 -0.0403 0.0474 -0.0579 174 LYS A C 1317 C C B LYS A 175 ? 0.8826 0.9233 0.9912 -0.0402 0.0474 -0.0579 174 LYS A C 1318 O O A LYS A 175 ? 0.8565 0.8996 0.9656 -0.0407 0.0448 -0.0549 174 LYS A O 1319 O O B LYS A 175 ? 0.8573 0.9002 0.9666 -0.0406 0.0447 -0.0548 174 LYS A O 1320 C CB A LYS A 175 ? 0.8563 0.8981 0.9590 -0.0414 0.0501 -0.0633 174 LYS A CB 1321 C CB B LYS A 175 ? 0.8582 0.8999 0.9610 -0.0414 0.0501 -0.0633 174 LYS A CB 1322 C CG A LYS A 175 ? 0.8556 0.8962 0.9551 -0.0412 0.0514 -0.0664 174 LYS A CG 1323 C CG B LYS A 175 ? 0.8549 0.8955 0.9545 -0.0412 0.0515 -0.0664 174 LYS A CG 1324 C CD A LYS A 175 ? 0.8811 0.9242 0.9777 -0.0429 0.0522 -0.0684 174 LYS A CD 1325 C CD B LYS A 175 ? 0.8694 0.9132 0.9663 -0.0421 0.0502 -0.0662 174 LYS A CD 1326 C CE A LYS A 175 ? 0.8822 0.9291 0.9782 -0.0436 0.0498 -0.0658 174 LYS A CE 1327 C CE B LYS A 175 ? 0.8845 0.9312 0.9808 -0.0440 0.0507 -0.0667 174 LYS A CE 1328 N NZ A LYS A 175 ? 0.8922 0.9417 0.9857 -0.0454 0.0506 -0.0677 174 LYS A NZ 1329 N NZ B LYS A 175 ? 0.8703 0.9204 0.9644 -0.0448 0.0491 -0.0657 174 LYS A NZ 1330 N N . LEU A 176 ? 0.9134 0.9524 1.0239 -0.0402 0.0492 -0.0589 175 LEU A N 1331 C CA . LEU A 176 ? 0.8862 0.9258 0.9998 -0.0406 0.0482 -0.0564 175 LEU A CA 1332 C C . LEU A 176 ? 0.9618 1.0003 1.0765 -0.0412 0.0510 -0.0586 175 LEU A C 1333 O O . LEU A 176 ? 1.0350 1.0713 1.1485 -0.0409 0.0535 -0.0617 175 LEU A O 1334 C CB . LEU A 176 ? 0.9921 1.0299 1.1084 -0.0391 0.0465 -0.0537 175 LEU A CB 1335 C CG . LEU A 176 ? 1.0248 1.0588 1.1416 -0.0373 0.0481 -0.0552 175 LEU A CG 1336 C CD1 . LEU A 176 ? 0.9350 0.9668 1.0538 -0.0371 0.0506 -0.0568 175 LEU A CD1 1337 C CD2 . LEU A 176 ? 0.9627 0.9958 1.0812 -0.0360 0.0455 -0.0522 175 LEU A CD2 1338 N N . PHE A 177 ? 1.1046 1.1444 1.2214 -0.0421 0.0504 -0.0567 176 PHE A N 1339 C CA . PHE A 177 ? 1.1191 1.1576 1.2376 -0.0424 0.0527 -0.0582 176 PHE A CA 1340 C C . PHE A 177 ? 1.1301 1.1661 1.2518 -0.0410 0.0524 -0.0565 176 PHE A C 1341 O O . PHE A 177 ? 1.1176 1.1545 1.2415 -0.0410 0.0500 -0.0531 176 PHE A O 1342 C CB . PHE A 177 ? 1.0079 1.0490 1.1270 -0.0441 0.0524 -0.0573 176 PHE A CB 1343 C CG . PHE A 177 ? 1.0529 1.0969 1.1690 -0.0455 0.0521 -0.0582 176 PHE A CG 1344 C CD1 . PHE A 177 ? 1.1585 1.2051 1.2740 -0.0459 0.0492 -0.0556 176 PHE A CD1 1345 C CD2 . PHE A 177 ? 1.1050 1.1491 1.2189 -0.0465 0.0546 -0.0617 176 PHE A CD2 1346 C CE1 . PHE A 177 ? 1.1659 1.2151 1.2788 -0.0471 0.0489 -0.0563 176 PHE A CE1 1347 C CE2 . PHE A 177 ? 1.1728 1.2197 1.2840 -0.0478 0.0543 -0.0625 176 PHE A CE2 1348 C CZ . PHE A 177 ? 1.1167 1.1662 1.2274 -0.0480 0.0515 -0.0598 176 PHE A CZ 1349 N N . PRO A 178 ? 1.1609 1.1936 1.2830 -0.0399 0.0546 -0.0586 177 PRO A N 1350 C CA . PRO A 178 ? 1.1661 1.1963 1.2912 -0.0384 0.0541 -0.0569 177 PRO A CA 1351 C C . PRO A 178 ? 1.2472 1.2778 1.3755 -0.0389 0.0539 -0.0550 177 PRO A C 1352 O O . PRO A 178 ? 1.1667 1.1982 1.2950 -0.0402 0.0554 -0.0561 177 PRO A O 1353 C CB . PRO A 178 ? 1.1069 1.1335 1.2314 -0.0374 0.0569 -0.0601 177 PRO A CB 1354 C CG . PRO A 178 ? 1.1976 1.2247 1.3187 -0.0385 0.0587 -0.0636 177 PRO A CG 1355 C CD . PRO A 178 ? 1.1773 1.2082 1.2974 -0.0402 0.0577 -0.0627 177 PRO A CD 1356 N N . THR A 179 ? 1.2939 1.3240 1.4247 -0.0380 0.0518 -0.0519 178 THR A N 1357 C CA . THR A 179 ? 1.3210 1.3514 1.4551 -0.0383 0.0511 -0.0496 178 THR A CA 1358 C C . THR A 179 ? 1.3422 1.3699 1.4789 -0.0366 0.0504 -0.0479 178 THR A C 1359 O O . THR A 179 ? 1.3347 1.3616 1.4709 -0.0354 0.0491 -0.0472 178 THR A O 1360 C CB . THR A 179 ? 1.3206 1.3540 1.4548 -0.0396 0.0480 -0.0465 178 THR A CB 1361 O OG1 . THR A 179 ? 1.3121 1.3480 1.4433 -0.0409 0.0480 -0.0477 178 THR A OG1 1362 C CG2 . THR A 179 ? 1.3169 1.3509 1.4537 -0.0405 0.0481 -0.0452 178 THR A CG2 1363 N N . ARG A 180 ? 1.3989 1.4255 1.5385 -0.0365 0.0515 -0.0474 179 ARG A N 1364 C CA . ARG A 180 ? 1.3787 1.4034 1.5212 -0.0351 0.0504 -0.0452 179 ARG A CA 1365 C C . ARG A 180 ? 1.3756 1.4017 1.5185 -0.0351 0.0464 -0.0416 179 ARG A C 1366 O O . ARG A 180 ? 1.3455 1.3700 1.4896 -0.0338 0.0450 -0.0401 179 ARG A O 1367 C CB . ARG A 180 ? 1.3928 1.4167 1.5384 -0.0353 0.0515 -0.0446 179 ARG A CB 1368 C CG . ARG A 180 ? 1.2852 1.3069 1.4309 -0.0350 0.0554 -0.0479 179 ARG A CG 1369 C CD . ARG A 180 ? 1.1850 1.2034 1.3313 -0.0331 0.0567 -0.0490 179 ARG A CD 1370 N NE . ARG A 180 ? 1.2166 1.2326 1.3628 -0.0330 0.0603 -0.0524 179 ARG A NE 1371 C CZ . ARG A 180 ? 1.3804 1.3956 1.5236 -0.0334 0.0623 -0.0558 179 ARG A CZ 1372 N NH1 . ARG A 180 ? 1.4009 1.4136 1.5440 -0.0335 0.0654 -0.0587 179 ARG A NH1 1373 N NH2 . ARG A 180 ? 1.3466 1.3635 1.4868 -0.0339 0.0611 -0.0562 179 ARG A NH2 1374 N N . PHE A 181 ? 1.3943 1.4233 1.5361 -0.0367 0.0445 -0.0403 180 PHE A N 1375 C CA . PHE A 181 ? 1.3721 1.4024 1.5137 -0.0371 0.0406 -0.0371 180 PHE A CA 1376 C C . PHE A 181 ? 1.3575 1.3873 1.4971 -0.0361 0.0394 -0.0372 180 PHE A C 1377 O O . PHE A 181 ? 1.3277 1.3574 1.4677 -0.0358 0.0363 -0.0346 180 PHE A O 1378 C CB . PHE A 181 ? 1.3998 1.4332 1.5404 -0.0391 0.0393 -0.0362 180 PHE A CB 1379 C CG . PHE A 181 ? 1.4716 1.5064 1.6111 -0.0397 0.0354 -0.0333 180 PHE A CG 1380 C CD1 . PHE A 181 ? 1.5232 1.5575 1.6647 -0.0398 0.0325 -0.0302 180 PHE A CD1 1381 C CD2 . PHE A 181 ? 1.3812 1.4178 1.5178 -0.0403 0.0346 -0.0339 180 PHE A CD2 1382 C CE1 . PHE A 181 ? 1.3922 1.4275 1.5325 -0.0405 0.0289 -0.0277 180 PHE A CE1 1383 C CE2 . PHE A 181 ? 1.4201 1.4578 1.5557 -0.0410 0.0310 -0.0313 180 PHE A CE2 1384 C CZ . PHE A 181 ? 1.3899 1.4269 1.5273 -0.0411 0.0281 -0.0282 180 PHE A CZ 1385 N N . ALA A 182 ? 1.2785 1.3078 1.4159 -0.0356 0.0417 -0.0402 181 ALA A N 1386 C CA . ALA A 182 ? 1.2327 1.2617 1.3679 -0.0348 0.0407 -0.0405 181 ALA A CA 1387 C C . ALA A 182 ? 1.1740 1.2000 1.3101 -0.0328 0.0413 -0.0409 181 ALA A C 1388 O O . ALA A 182 ? 1.0892 1.1147 1.2238 -0.0320 0.0402 -0.0408 181 ALA A O 1389 C CB . ALA A 182 ? 1.1069 1.1371 1.2389 -0.0354 0.0426 -0.0435 181 ALA A CB 1390 N N . ARG A 183 ? 1.1001 1.1239 1.2387 -0.0319 0.0431 -0.0414 182 ARG A N 1391 C CA . ARG A 183 ? 1.1590 1.1798 1.2985 -0.0299 0.0437 -0.0419 182 ARG A CA 1392 C C . ARG A 183 ? 1.1043 1.1248 1.2455 -0.0292 0.0403 -0.0384 182 ARG A C 1393 O O . ARG A 183 ? 1.0797 1.1016 1.2223 -0.0302 0.0380 -0.0357 182 ARG A O 1394 C CB . ARG A 183 ? 1.2073 1.2256 1.3487 -0.0291 0.0469 -0.0437 182 ARG A CB 1395 C CG . ARG A 183 ? 1.2030 1.2202 1.3481 -0.0282 0.0459 -0.0413 182 ARG A CG 1396 C CD . ARG A 183 ? 1.1813 1.1954 1.3279 -0.0271 0.0492 -0.0434 182 ARG A CD 1397 N NE . ARG A 183 ? 1.1648 1.1792 1.3114 -0.0282 0.0519 -0.0455 182 ARG A NE 1398 C CZ . ARG A 183 ? 0.9794 0.9912 1.1270 -0.0276 0.0549 -0.0477 182 ARG A CZ 1399 N NH1 . ARG A 183 ? 0.9672 0.9760 1.1160 -0.0258 0.0557 -0.0481 182 ARG A NH1 1400 N NH2 . ARG A 183 ? 1.0542 1.0663 1.2016 -0.0288 0.0572 -0.0496 182 ARG A NH2 1401 N N . GLY A 184 ? 1.1321 1.1507 1.2731 -0.0276 0.0400 -0.0384 183 GLY A N 1402 C CA . GLY A 184 ? 1.0159 1.0343 1.1576 -0.0271 0.0364 -0.0354 183 GLY A CA 1403 C C . GLY A 184 ? 0.9499 0.9701 1.0889 -0.0280 0.0338 -0.0344 183 GLY A C 1404 O O . GLY A 184 ? 0.8813 0.9007 1.0199 -0.0273 0.0312 -0.0326 183 GLY A O 1405 N N . ARG A 185 ? 0.9519 0.9745 1.0888 -0.0296 0.0343 -0.0354 184 ARG A N 1406 C CA . ARG A 185 ? 0.9321 0.9565 1.0663 -0.0304 0.0320 -0.0346 184 ARG A CA 1407 C C . ARG A 185 ? 0.8696 0.8929 1.0018 -0.0291 0.0327 -0.0363 184 ARG A C 1408 O O . ARG A 185 ? 0.8682 0.8900 1.0001 -0.0280 0.0358 -0.0390 184 ARG A O 1409 C CB . ARG A 185 ? 1.0157 1.0429 1.1481 -0.0323 0.0328 -0.0357 184 ARG A CB 1410 C CG . ARG A 185 ? 1.0407 1.0695 1.1746 -0.0338 0.0320 -0.0341 184 ARG A CG 1411 C CD . ARG A 185 ? 1.0404 1.0692 1.1755 -0.0343 0.0280 -0.0304 184 ARG A CD 1412 N NE . ARG A 185 ? 1.1651 1.1915 1.3031 -0.0332 0.0280 -0.0294 184 ARG A NE 1413 C CZ . ARG A 185 ? 1.1902 1.2167 1.3305 -0.0338 0.0279 -0.0282 184 ARG A CZ 1414 N NH1 . ARG A 185 ? 1.2752 1.3040 1.4153 -0.0355 0.0278 -0.0279 184 ARG A NH1 1415 N NH2 . ARG A 185 ? 1.0490 1.0735 1.1921 -0.0326 0.0280 -0.0273 184 ARG A NH2 1416 N N . ARG A 186 ? 0.8117 0.8356 0.9422 -0.0294 0.0298 -0.0346 185 ARG A N 1417 C CA . ARG A 186 ? 0.8353 0.8585 0.9635 -0.0284 0.0300 -0.0359 185 ARG A CA 1418 C C . ARG A 186 ? 0.7635 0.7893 0.8888 -0.0297 0.0296 -0.0365 185 ARG A C 1419 O O . ARG A 186 ? 0.7640 0.7918 0.8889 -0.0312 0.0270 -0.0344 185 ARG A O 1420 C CB . ARG A 186 ? 0.7585 0.7800 0.8870 -0.0274 0.0269 -0.0336 185 ARG A CB 1421 C CG . ARG A 186 ? 0.6780 0.6990 0.8042 -0.0264 0.0268 -0.0346 185 ARG A CG 1422 C CD . ARG A 186 ? 0.6208 0.6400 0.7472 -0.0257 0.0234 -0.0321 185 ARG A CD 1423 N NE . ARG A 186 ? 0.6309 0.6478 0.7601 -0.0243 0.0235 -0.0313 185 ARG A NE 1424 C CZ . ARG A 186 ? 0.7251 0.7400 0.8551 -0.0223 0.0256 -0.0329 185 ARG A CZ 1425 N NH1 . ARG A 186 ? 0.6661 0.6791 0.7987 -0.0211 0.0256 -0.0320 185 ARG A NH1 1426 N NH2 . ARG A 186 ? 0.6463 0.6611 0.7743 -0.0216 0.0279 -0.0355 185 ARG A NH2 1427 N N . ILE A 187 ? 0.7151 0.7410 0.8384 -0.0293 0.0322 -0.0395 186 ILE A N 1428 C CA . ILE A 187 ? 0.7659 0.7941 0.8863 -0.0303 0.0319 -0.0402 186 ILE A CA 1429 C C . ILE A 187 ? 0.6658 0.6929 0.7845 -0.0292 0.0306 -0.0400 186 ILE A C 1430 O O . ILE A 187 ? 0.6765 0.7010 0.7957 -0.0274 0.0316 -0.0409 186 ILE A O 1431 C CB . ILE A 187 ? 0.8231 0.8519 0.9419 -0.0307 0.0355 -0.0438 186 ILE A CB 1432 C CG1 . ILE A 187 ? 0.7552 0.7809 0.8745 -0.0291 0.0385 -0.0465 186 ILE A CG1 1433 C CG2 . ILE A 187 ? 0.9101 0.9409 1.0297 -0.0323 0.0362 -0.0438 186 ILE A CG2 1434 C CD1 . ILE A 187 ? 0.8343 0.8601 0.9514 -0.0296 0.0416 -0.0502 186 ILE A CD1 1435 N N . THR A 188 ? 0.6422 0.6712 0.7589 -0.0301 0.0283 -0.0387 187 THR A N 1436 C CA . THR A 188 ? 0.6286 0.6567 0.7438 -0.0293 0.0265 -0.0379 187 THR A CA 1437 C C . THR A 188 ? 0.5681 0.5983 0.6803 -0.0299 0.0270 -0.0393 187 THR A C 1438 O O . THR A 188 ? 0.5402 0.5731 0.6515 -0.0316 0.0264 -0.0388 187 THR A O 1439 C CB . THR A 188 ? 0.5551 0.5828 0.6709 -0.0297 0.0222 -0.0343 187 THR A CB 1440 O OG1 . THR A 188 ? 0.6603 0.6859 0.7788 -0.0290 0.0218 -0.0331 187 THR A OG1 1441 C CG2 . THR A 188 ? 0.4695 0.4958 0.5834 -0.0289 0.0202 -0.0335 187 THR A CG2 1442 N N . CYS A 189 ? 0.6004 0.6293 0.7110 -0.0286 0.0282 -0.0410 188 CYS A N 1443 C CA . CYS A 189 ? 0.6299 0.6605 0.7376 -0.0290 0.0283 -0.0420 188 CYS A CA 1444 C C . CYS A 189 ? 0.5100 0.5402 0.6168 -0.0288 0.0248 -0.0395 188 CYS A C 1445 O O . CYS A 189 ? 0.5073 0.5349 0.6149 -0.0274 0.0237 -0.0386 188 CYS A O 1446 C CB . CYS A 189 ? 0.4966 0.5257 0.6027 -0.0278 0.0316 -0.0456 188 CYS A CB 1447 S SG . CYS A 189 ? 0.8890 0.9203 0.9915 -0.0284 0.0314 -0.0466 188 CYS A SG 1448 N N . VAL A 190 ? 0.4443 0.4769 0.5493 -0.0302 0.0230 -0.0383 189 VAL A N 1449 C CA . VAL A 190 ? 0.4049 0.4372 0.5086 -0.0303 0.0196 -0.0360 189 VAL A CA 1450 C C . VAL A 190 ? 0.4469 0.4809 0.5479 -0.0304 0.0205 -0.0375 189 VAL A C 1451 O O . VAL A 190 ? 0.4919 0.5286 0.5918 -0.0316 0.0216 -0.0384 189 VAL A O 1452 C CB . VAL A 190 ? 0.4396 0.4730 0.5435 -0.0320 0.0160 -0.0329 189 VAL A CB 1453 C CG1 . VAL A 190 ? 0.3286 0.3613 0.4304 -0.0323 0.0124 -0.0307 189 VAL A CG1 1454 C CG2 . VAL A 190 ? 0.4950 0.5267 0.6014 -0.0320 0.0151 -0.0315 189 VAL A CG2 1455 N N A VAL A 191 ? 0.4192 0.4515 0.5189 -0.0291 0.0199 -0.0376 190 VAL A N 1456 N N B VAL A 191 ? 0.4185 0.4508 0.5183 -0.0291 0.0203 -0.0379 190 VAL A N 1457 C CA A VAL A 191 ? 0.4049 0.4384 0.5020 -0.0290 0.0209 -0.0391 190 VAL A CA 1458 C CA B VAL A 191 ? 0.4118 0.4455 0.5089 -0.0291 0.0209 -0.0391 190 VAL A CA 1459 C C A VAL A 191 ? 0.3607 0.3939 0.4563 -0.0293 0.0172 -0.0366 190 VAL A C 1460 C C B VAL A 191 ? 0.3669 0.4002 0.4627 -0.0294 0.0171 -0.0364 190 VAL A C 1461 O O A VAL A 191 ? 0.3489 0.3793 0.4448 -0.0283 0.0153 -0.0352 190 VAL A O 1462 O O B VAL A 191 ? 0.3766 0.4071 0.4730 -0.0287 0.0147 -0.0346 190 VAL A O 1463 C CB A VAL A 191 ? 0.4127 0.4441 0.5094 -0.0271 0.0239 -0.0420 190 VAL A CB 1464 C CB B VAL A 191 ? 0.4083 0.4402 0.5045 -0.0273 0.0240 -0.0422 190 VAL A CB 1465 C CG1 A VAL A 191 ? 0.4235 0.4558 0.5174 -0.0269 0.0246 -0.0434 190 VAL A CG1 1466 C CG1 B VAL A 191 ? 0.4202 0.4507 0.5183 -0.0266 0.0269 -0.0443 190 VAL A CG1 1467 C CG2 A VAL A 191 ? 0.4219 0.4530 0.5195 -0.0270 0.0274 -0.0448 190 VAL A CG2 1468 C CG2 B VAL A 191 ? 0.3951 0.4245 0.4910 -0.0258 0.0225 -0.0413 190 VAL A CG2 1469 N N . LYS A 192 ? 0.3321 0.3680 0.4260 -0.0306 0.0163 -0.0360 191 LYS A N 1470 C CA . LYS A 192 ? 0.3923 0.4280 0.4845 -0.0311 0.0128 -0.0337 191 LYS A CA 1471 C C . LYS A 192 ? 0.4313 0.4676 0.5212 -0.0303 0.0140 -0.0352 191 LYS A C 1472 O O . LYS A 192 ? 0.3652 0.4038 0.4543 -0.0305 0.0168 -0.0375 191 LYS A O 1473 C CB . LYS A 192 ? 0.2969 0.3351 0.3887 -0.0331 0.0106 -0.0316 191 LYS A CB 1474 C CG . LYS A 192 ? 0.4126 0.4505 0.5065 -0.0339 0.0096 -0.0302 191 LYS A CG 1475 C CD . LYS A 192 ? 0.3608 0.4017 0.4545 -0.0358 0.0086 -0.0290 191 LYS A CD 1476 C CE . LYS A 192 ? 0.3977 0.4381 0.4936 -0.0365 0.0079 -0.0279 191 LYS A CE 1477 N NZ . LYS A 192 ? 0.4334 0.4707 0.5292 -0.0365 0.0044 -0.0254 191 LYS A NZ 1478 N N . HIS A 193 ? 0.3979 0.4319 0.4866 -0.0296 0.0118 -0.0340 192 HIS A N 1479 C CA . HIS A 193 ? 0.3478 0.3822 0.4344 -0.0289 0.0127 -0.0352 192 HIS A CA 1480 C C . HIS A 193 ? 0.3628 0.3948 0.4478 -0.0287 0.0091 -0.0330 192 HIS A C 1481 O O . HIS A 193 ? 0.3881 0.4165 0.4735 -0.0281 0.0070 -0.0317 192 HIS A O 1482 C CB . HIS A 193 ? 0.3860 0.4190 0.4729 -0.0270 0.0163 -0.0383 192 HIS A CB 1483 C CG . HIS A 193 ? 0.4125 0.4462 0.4971 -0.0263 0.0177 -0.0399 192 HIS A CG 1484 N ND1 . HIS A 193 ? 0.4029 0.4342 0.4866 -0.0251 0.0165 -0.0394 192 HIS A ND1 1485 C CD2 . HIS A 193 ? 0.3985 0.4348 0.4815 -0.0268 0.0200 -0.0420 192 HIS A CD2 1486 C CE1 . HIS A 193 ? 0.3713 0.4038 0.4530 -0.0248 0.0181 -0.0410 192 HIS A CE1 1487 N NE2 . HIS A 193 ? 0.3912 0.4267 0.4723 -0.0258 0.0203 -0.0427 192 HIS A NE2 1488 N N . PRO A 194 ? 0.3638 0.3972 0.4466 -0.0292 0.0081 -0.0326 193 PRO A N 1489 C CA . PRO A 194 ? 0.3816 0.4122 0.4622 -0.0292 0.0044 -0.0305 193 PRO A CA 1490 C C . PRO A 194 ? 0.3946 0.4210 0.4747 -0.0273 0.0044 -0.0311 193 PRO A C 1491 O O . PRO A 194 ? 0.3595 0.3824 0.4388 -0.0272 0.0013 -0.0301 193 PRO A O 1492 C CB . PRO A 194 ? 0.2784 0.3120 0.3571 -0.0299 0.0044 -0.0305 193 PRO A CB 1493 C CG . PRO A 194 ? 0.3048 0.3418 0.3843 -0.0297 0.0085 -0.0331 193 PRO A CG 1494 C CD . PRO A 194 ? 0.3539 0.3914 0.4358 -0.0299 0.0101 -0.0338 193 PRO A CD 1495 N N . ALA A 195 ? 0.3746 0.4010 0.4561 -0.0257 0.0080 -0.0337 194 ALA A N 1496 C CA . ALA A 195 ? 0.3231 0.3456 0.4058 -0.0237 0.0083 -0.0351 194 ALA A CA 1497 C C . ALA A 195 ? 0.4374 0.4566 0.5219 -0.0232 0.0070 -0.0341 194 ALA A C 1498 O O . ALA A 195 ? 0.4426 0.4580 0.5283 -0.0215 0.0066 -0.0348 194 ALA A O 1499 C CB . ALA A 195 ? 0.3234 0.3469 0.4068 -0.0221 0.0127 -0.0383 194 ALA A CB 1500 N N . LEU A 196 ? 0.3855 0.4059 0.4700 -0.0245 0.0062 -0.0324 195 LEU A N 1501 C CA . LEU A 196 ? 0.4141 0.4318 0.5003 -0.0241 0.0052 -0.0314 195 LEU A CA 1502 C C . LEU A 196 ? 0.5166 0.5315 0.6013 -0.0252 0.0007 -0.0288 195 LEU A C 1503 O O . LEU A 196 ? 0.4422 0.4591 0.5251 -0.0270 -0.0012 -0.0273 195 LEU A O 1504 C CB . LEU A 196 ? 0.3773 0.3979 0.4663 -0.0247 0.0079 -0.0324 195 LEU A CB 1505 C CG . LEU A 196 ? 0.4387 0.4614 0.5289 -0.0236 0.0127 -0.0357 195 LEU A CG 1506 C CD1 . LEU A 196 ? 0.3716 0.3968 0.4637 -0.0244 0.0150 -0.0368 195 LEU A CD1 1507 C CD2 . LEU A 196 ? 0.4371 0.4569 0.5283 -0.0213 0.0143 -0.0370 195 LEU A CD2 1508 N N . GLU A 197 ? 0.4821 0.4923 0.5677 -0.0239 -0.0010 -0.0284 196 GLU A N 1509 C CA . GLU A 197 ? 0.5549 0.5617 0.6389 -0.0246 -0.0052 -0.0261 196 GLU A CA 1510 C C . GLU A 197 ? 0.5059 0.5147 0.5900 -0.0263 -0.0056 -0.0245 196 GLU A C 1511 O O . GLU A 197 ? 0.4985 0.5072 0.5810 -0.0278 -0.0082 -0.0227 196 GLU A O 1512 C CB . GLU A 197 ? 0.6163 0.6173 0.7008 -0.0225 -0.0067 -0.0260 196 GLU A CB 1513 C CG . GLU A 197 ? 0.8363 0.8325 0.9182 -0.0224 -0.0113 -0.0240 196 GLU A CG 1514 C CD . GLU A 197 ? 0.9029 0.8953 0.9854 -0.0215 -0.0130 -0.0226 196 GLU A CD 1515 O OE1 . GLU A 197 ? 0.8685 0.8621 0.9537 -0.0211 -0.0107 -0.0232 196 GLU A OE1 1516 O OE2 . GLU A 197 ? 0.7669 0.7551 0.8473 -0.0210 -0.0166 -0.0209 196 GLU A OE2 1517 N N . LYS A 198 ? 0.3927 0.4034 0.4803 -0.0259 -0.0027 -0.0255 197 LYS A N 1518 C CA . LYS A 198 ? 0.3896 0.4029 0.4797 -0.0271 -0.0022 -0.0250 197 LYS A CA 1519 C C . LYS A 198 ? 0.3309 0.3484 0.4234 -0.0271 0.0020 -0.0272 197 LYS A C 1520 O O . LYS A 198 ? 0.3726 0.3905 0.4654 -0.0258 0.0048 -0.0292 197 LYS A O 1521 C CB . LYS A 198 ? 0.4876 0.4977 0.5794 -0.0264 -0.0032 -0.0241 197 LYS A CB 1522 C CG . LYS A 198 ? 0.6306 0.6368 0.7199 -0.0267 -0.0074 -0.0219 197 LYS A CG 1523 C CD . LYS A 198 ? 0.7035 0.7046 0.7925 -0.0247 -0.0086 -0.0215 197 LYS A CD 1524 C CE . LYS A 198 ? 0.6958 0.6935 0.7839 -0.0249 -0.0122 -0.0194 197 LYS A CE 1525 N NZ . LYS A 198 ? 0.6830 0.6763 0.7715 -0.0230 -0.0132 -0.0189 197 LYS A NZ 1526 N N . ASP A 199 ? 0.3537 0.3740 0.4478 -0.0284 0.0027 -0.0269 198 ASP A N 1527 C CA . ASP A 199 ? 0.3515 0.3749 0.4478 -0.0283 0.0068 -0.0292 198 ASP A CA 1528 C C . ASP A 199 ? 0.4353 0.4568 0.5340 -0.0265 0.0092 -0.0306 198 ASP A C 1529 O O . ASP A 199 ? 0.4214 0.4402 0.5213 -0.0259 0.0077 -0.0294 198 ASP A O 1530 C CB . ASP A 199 ? 0.4334 0.4594 0.5308 -0.0301 0.0066 -0.0283 198 ASP A CB 1531 C CG . ASP A 199 ? 0.4610 0.4892 0.5563 -0.0319 0.0043 -0.0268 198 ASP A CG 1532 O OD1 . ASP A 199 ? 0.4325 0.4608 0.5256 -0.0317 0.0036 -0.0269 198 ASP A OD1 1533 O OD2 . ASP A 199 ? 0.4475 0.4774 0.5435 -0.0334 0.0034 -0.0256 198 ASP A OD2 1534 N N . ILE A 200 ? 0.4471 0.4699 0.5463 -0.0255 0.0131 -0.0334 199 ILE A N 1535 C CA . ILE A 200 ? 0.4399 0.4612 0.5413 -0.0239 0.0160 -0.0352 199 ILE A CA 1536 C C . ILE A 200 ? 0.4810 0.5037 0.5846 -0.0248 0.0173 -0.0354 199 ILE A C 1537 O O . ILE A 200 ? 0.4418 0.4673 0.5448 -0.0263 0.0178 -0.0356 199 ILE A O 1538 C CB . ILE A 200 ? 0.3903 0.4120 0.4908 -0.0226 0.0197 -0.0384 199 ILE A CB 1539 C CG1 . ILE A 200 ? 0.4247 0.4448 0.5235 -0.0215 0.0183 -0.0381 199 ILE A CG1 1540 C CG2 . ILE A 200 ? 0.4095 0.4297 0.5121 -0.0211 0.0230 -0.0406 199 ILE A CG2 1541 C CD1 . ILE A 200 ? 0.3031 0.3237 0.4004 -0.0204 0.0216 -0.0411 199 ILE A CD1 1542 N N . ARG A 201 ? 0.4354 0.4561 0.5415 -0.0238 0.0178 -0.0352 200 ARG A N 1543 C CA . ARG A 201 ? 0.4655 0.4870 0.5737 -0.0245 0.0190 -0.0353 200 ARG A CA 1544 C C . ARG A 201 ? 0.4907 0.5106 0.6010 -0.0228 0.0224 -0.0375 200 ARG A C 1545 O O . ARG A 201 ? 0.5139 0.5312 0.6253 -0.0212 0.0220 -0.0370 200 ARG A O 1546 C CB . ARG A 201 ? 0.4542 0.4749 0.5634 -0.0255 0.0153 -0.0321 200 ARG A CB 1547 C CG . ARG A 201 ? 0.4288 0.4512 0.5359 -0.0274 0.0123 -0.0302 200 ARG A CG 1548 C CD . ARG A 201 ? 0.4578 0.4783 0.5651 -0.0282 0.0083 -0.0272 200 ARG A CD 1549 N NE . ARG A 201 ? 0.3973 0.4198 0.5030 -0.0302 0.0062 -0.0257 200 ARG A NE 1550 C CZ . ARG A 201 ? 0.4885 0.5132 0.5956 -0.0316 0.0066 -0.0253 200 ARG A CZ 1551 N NH1 . ARG A 201 ? 0.4827 0.5075 0.5925 -0.0311 0.0089 -0.0262 200 ARG A NH1 1552 N NH2 . ARG A 201 ? 0.4775 0.5042 0.5831 -0.0334 0.0047 -0.0240 200 ARG A NH2 1553 N N . TYR A 202 ? 0.4144 0.4355 0.5251 -0.0232 0.0256 -0.0398 201 TYR A N 1554 C CA . TYR A 202 ? 0.5467 0.5659 0.6592 -0.0220 0.0287 -0.0418 201 TYR A CA 1555 C C . TYR A 202 ? 0.5654 0.5859 0.6794 -0.0233 0.0296 -0.0418 201 TYR A C 1556 O O . TYR A 202 ? 0.5580 0.5810 0.6708 -0.0249 0.0298 -0.0422 201 TYR A O 1557 C CB . TYR A 202 ? 0.4836 0.5017 0.5943 -0.0209 0.0323 -0.0456 201 TYR A CB 1558 C CG . TYR A 202 ? 0.4913 0.5080 0.6007 -0.0194 0.0318 -0.0459 201 TYR A CG 1559 C CD1 . TYR A 202 ? 0.5627 0.5771 0.6738 -0.0176 0.0309 -0.0447 201 TYR A CD1 1560 C CD2 . TYR A 202 ? 0.5233 0.5410 0.6296 -0.0198 0.0322 -0.0472 201 TYR A CD2 1561 C CE1 . TYR A 202 ? 0.6401 0.6532 0.7500 -0.0162 0.0305 -0.0449 201 TYR A CE1 1562 C CE2 . TYR A 202 ? 0.4955 0.5118 0.6006 -0.0183 0.0318 -0.0474 201 TYR A CE2 1563 C CZ . TYR A 202 ? 0.6255 0.6395 0.7324 -0.0165 0.0309 -0.0462 201 TYR A CZ 1564 O OH . TYR A 202 ? 0.6951 0.7079 0.8011 -0.0150 0.0305 -0.0463 201 TYR A OH 1565 N N . SER A 203 ? 0.5181 0.5369 0.6349 -0.0225 0.0300 -0.0413 202 SER A N 1566 C CA . SER A 203 ? 0.5553 0.5751 0.6740 -0.0236 0.0306 -0.0409 202 SER A CA 1567 C C . SER A 203 ? 0.5301 0.5475 0.6509 -0.0223 0.0334 -0.0426 202 SER A C 1568 O O . SER A 203 ? 0.6161 0.6310 0.7373 -0.0205 0.0342 -0.0434 202 SER A O 1569 C CB . SER A 203 ? 0.6013 0.6214 0.7214 -0.0245 0.0268 -0.0372 202 SER A CB 1570 O OG . SER A 203 ? 0.6817 0.6993 0.8035 -0.0230 0.0255 -0.0358 202 SER A OG 1571 N N . PHE A 204 ? 0.6167 0.6347 0.7387 -0.0232 0.0350 -0.0433 203 PHE A N 1572 C CA . PHE A 204 ? 0.7184 0.7340 0.8426 -0.0222 0.0373 -0.0444 203 PHE A CA 1573 C C . PHE A 204 ? 0.7805 0.7976 0.9066 -0.0236 0.0375 -0.0437 203 PHE A C 1574 O O . PHE A 204 ? 0.7846 0.8042 0.9096 -0.0253 0.0370 -0.0434 203 PHE A O 1575 C CB . PHE A 204 ? 0.7682 0.7816 0.8910 -0.0213 0.0409 -0.0483 203 PHE A CB 1576 C CG . PHE A 204 ? 0.7295 0.7443 0.8500 -0.0229 0.0429 -0.0509 203 PHE A CG 1577 C CD1 . PHE A 204 ? 0.6625 0.6786 0.7799 -0.0234 0.0428 -0.0521 203 PHE A CD1 1578 C CD2 . PHE A 204 ? 0.7666 0.7813 0.8881 -0.0238 0.0449 -0.0521 203 PHE A CD2 1579 C CE1 . PHE A 204 ? 0.7691 0.7865 0.8843 -0.0249 0.0445 -0.0544 203 PHE A CE1 1580 C CE2 . PHE A 204 ? 0.7495 0.7655 0.8690 -0.0253 0.0467 -0.0545 203 PHE A CE2 1581 C CZ . PHE A 204 ? 0.8035 0.8209 0.9198 -0.0259 0.0465 -0.0557 203 PHE A CZ 1582 N N . ILE A 205 ? 0.7935 0.8087 0.9224 -0.0227 0.0384 -0.0433 204 ILE A N 1583 C CA . ILE A 205 ? 0.8513 0.8674 0.9822 -0.0238 0.0387 -0.0426 204 ILE A CA 1584 C C . ILE A 205 ? 0.8278 0.8439 0.9577 -0.0246 0.0423 -0.0459 204 ILE A C 1585 O O . ILE A 205 ? 0.7315 0.7450 0.8608 -0.0235 0.0450 -0.0486 204 ILE A O 1586 C CB . ILE A 205 ? 0.9182 0.9323 1.0525 -0.0226 0.0384 -0.0410 204 ILE A CB 1587 C CG1 . ILE A 205 ? 0.8933 0.9070 1.0283 -0.0219 0.0349 -0.0380 204 ILE A CG1 1588 C CG2 . ILE A 205 ? 0.8637 0.8788 1.0002 -0.0238 0.0385 -0.0399 204 ILE A CG2 1589 C CD1 . ILE A 205 ? 0.7616 0.7773 0.8967 -0.0236 0.0312 -0.0348 204 ILE A CD1 1590 N N . LEU A 206 ? 0.8583 0.8769 0.9877 -0.0264 0.0421 -0.0457 205 LEU A N 1591 C CA . LEU A 206 ? 0.7840 0.8028 0.9128 -0.0273 0.0452 -0.0485 205 LEU A CA 1592 C C . LEU A 206 ? 0.9084 0.9246 1.0398 -0.0266 0.0473 -0.0493 205 LEU A C 1593 O O . LEU A 206 ? 0.9447 0.9608 1.0790 -0.0263 0.0460 -0.0468 205 LEU A O 1594 C CB . LEU A 206 ? 0.7923 0.8143 0.9206 -0.0294 0.0443 -0.0476 205 LEU A CB 1595 C CG . LEU A 206 ? 0.9528 0.9774 1.0781 -0.0305 0.0433 -0.0480 205 LEU A CG 1596 C CD1 . LEU A 206 ? 0.8753 0.9029 1.0003 -0.0324 0.0429 -0.0474 205 LEU A CD1 1597 C CD2 . LEU A 206 ? 0.9142 0.9375 1.0367 -0.0300 0.0459 -0.0517 205 LEU A CD2 1598 N N . ASP A 207 ? 0.9492 0.9633 1.0796 -0.0263 0.0504 -0.0527 206 ASP A N 1599 C CA . ASP A 207 ? 0.9541 0.9657 1.0867 -0.0258 0.0527 -0.0538 206 ASP A CA 1600 C C . ASP A 207 ? 1.0464 1.0589 1.1780 -0.0275 0.0548 -0.0560 206 ASP A C 1601 O O . ASP A 207 ? 1.0471 1.0591 1.1760 -0.0281 0.0566 -0.0591 206 ASP A O 1602 C CB . ASP A 207 ? 0.9022 0.9098 1.0343 -0.0242 0.0546 -0.0561 206 ASP A CB 1603 C CG . ASP A 207 ? 0.9311 0.9358 1.0659 -0.0233 0.0564 -0.0564 206 ASP A CG 1604 O OD1 . ASP A 207 ? 1.0064 1.0122 1.1431 -0.0242 0.0567 -0.0555 206 ASP A OD1 1605 O OD2 . ASP A 207 ? 0.9310 0.9322 1.0661 -0.0218 0.0574 -0.0575 206 ASP A OD2 1606 N N . ILE A 208 ? 1.2007 1.2148 1.3345 -0.0285 0.0545 -0.0544 207 ILE A N 1607 C CA . ILE A 208 ? 1.2442 1.2590 1.3775 -0.0300 0.0566 -0.0564 207 ILE A CA 1608 C C . ILE A 208 ? 1.1894 1.2015 1.3254 -0.0294 0.0588 -0.0571 207 ILE A C 1609 O O . ILE A 208 ? 1.2020 1.2137 1.3411 -0.0286 0.0577 -0.0545 207 ILE A O 1610 C CB . ILE A 208 ? 1.1645 1.1832 1.2980 -0.0317 0.0550 -0.0545 207 ILE A CB 1611 C CG1 . ILE A 208 ? 1.2326 1.2517 1.3654 -0.0332 0.0575 -0.0570 207 ILE A CG1 1612 C CG2 . ILE A 208 ? 1.2101 1.2296 1.3468 -0.0316 0.0529 -0.0509 207 ILE A CG2 1613 C CD1 . ILE A 208 ? 1.2375 1.2596 1.3708 -0.0348 0.0565 -0.0555 207 ILE A CD1 1614 N N . GLN A 209 ? 1.1666 1.1767 1.3014 -0.0299 0.0617 -0.0606 208 GLN A N 1615 C CA . GLN A 209 ? 1.1026 1.1092 1.2393 -0.0292 0.0641 -0.0619 208 GLN A CA 1616 C C . GLN A 209 ? 1.1041 1.1078 1.2424 -0.0271 0.0636 -0.0608 208 GLN A C 1617 O O . GLN A 209 ? 1.0499 1.0536 1.1869 -0.0262 0.0621 -0.0602 208 GLN A O 1618 C CB . GLN A 209 ? 1.1616 1.1693 1.3011 -0.0299 0.0645 -0.0605 208 GLN A CB 1619 C CG . GLN A 209 ? 1.1713 1.1753 1.3131 -0.0290 0.0668 -0.0615 208 GLN A CG 1620 C CD . GLN A 209 ? 0.9765 0.9815 1.1214 -0.0295 0.0670 -0.0598 208 GLN A CD 1621 O OE1 . GLN A 209 ? 0.9965 1.0019 1.1411 -0.0309 0.0688 -0.0615 208 GLN A OE1 1622 N NE2 . GLN A 209 ? 0.8511 0.8565 0.9990 -0.0285 0.0651 -0.0565 208 GLN A NE2 1623 N N . PRO B 1 ? 0.6190 0.6231 0.6090 0.0119 0.0239 -0.0308 0 PRO B N 1624 C CA . PRO B 1 ? 0.7083 0.7074 0.6984 0.0136 0.0235 -0.0300 0 PRO B CA 1625 C C . PRO B 1 ? 0.6825 0.6746 0.6674 0.0179 0.0223 -0.0277 0 PRO B C 1626 O O . PRO B 1 ? 0.5012 0.4962 0.4855 0.0184 0.0231 -0.0265 0 PRO B O 1627 C CB . PRO B 1 ? 0.6210 0.6148 0.6111 0.0141 0.0216 -0.0314 0 PRO B CB 1628 C CG . PRO B 1 ? 0.5957 0.5957 0.5882 0.0111 0.0211 -0.0335 0 PRO B CG 1629 C CD . PRO B 1 ? 0.4560 0.4642 0.4489 0.0092 0.0223 -0.0323 0 PRO B CD 1630 N N . SER B 2 ? 0.7135 0.6999 0.6976 0.0201 0.0187 -0.0280 1 SER B N 1631 C CA . SER B 2 ? 0.6350 0.6200 0.6232 0.0193 0.0173 -0.0287 1 SER B CA 1632 C C . SER B 2 ? 0.6162 0.5918 0.5989 0.0203 0.0174 -0.0263 1 SER B C 1633 O O . SER B 2 ? 0.5603 0.5296 0.5409 0.0215 0.0157 -0.0237 1 SER B O 1634 C CB . SER B 2 ? 0.6048 0.5878 0.5962 0.0193 0.0152 -0.0287 1 SER B CB 1635 O OG . SER B 2 ? 0.6655 0.6441 0.6569 0.0191 0.0145 -0.0290 1 SER B OG 1636 N N . ILE B 3 ? 0.5780 0.5528 0.5565 0.0206 0.0179 -0.0261 2 ILE B N 1637 C CA . ILE B 3 ? 0.4955 0.4624 0.4663 0.0231 0.0157 -0.0231 2 ILE B CA 1638 C C . ILE B 3 ? 0.5114 0.4823 0.4797 0.0233 0.0177 -0.0221 2 ILE B C 1639 O O . ILE B 3 ? 0.5919 0.5722 0.5627 0.0207 0.0189 -0.0227 2 ILE B O 1640 C CB . ILE B 3 ? 0.4942 0.4606 0.4635 0.0223 0.0133 -0.0230 2 ILE B CB 1641 C CG1 . ILE B 3 ? 0.6280 0.5937 0.6009 0.0217 0.0131 -0.0256 2 ILE B CG1 1642 C CG2 . ILE B 3 ? 0.4458 0.4032 0.4094 0.0240 0.0091 -0.0193 2 ILE B CG2 1643 C CD1 . ILE B 3 ? 0.5599 0.5169 0.5320 0.0230 0.0103 -0.0238 2 ILE B CD1 1644 N N . ILE B 4 ? 0.4929 0.4598 0.4593 0.0246 0.0170 -0.0195 3 ILE B N 1645 C CA . ILE B 4 ? 0.4858 0.4566 0.4507 0.0246 0.0189 -0.0184 3 ILE B CA 1646 C C . ILE B 4 ? 0.4735 0.4389 0.4307 0.0269 0.0173 -0.0155 3 ILE B C 1647 O O . ILE B 4 ? 0.4658 0.4214 0.4182 0.0293 0.0147 -0.0129 3 ILE B O 1648 C CB . ILE B 4 ? 0.5114 0.4815 0.4787 0.0245 0.0191 -0.0174 3 ILE B CB 1649 C CG1 . ILE B 4 ? 0.5268 0.5042 0.5020 0.0219 0.0202 -0.0206 3 ILE B CG1 1650 C CG2 . ILE B 4 ? 0.4914 0.4642 0.4566 0.0248 0.0205 -0.0159 3 ILE B CG2 1651 C CD1 . ILE B 4 ? 0.6121 0.6006 0.5916 0.0195 0.0225 -0.0236 3 ILE B CD1 1652 N N . VAL B 5 ? 0.4640 0.4395 0.4240 0.0235 0.0172 -0.0144 4 VAL B N 1653 C CA . VAL B 5 ? 0.4269 0.4021 0.3842 0.0228 0.0143 -0.0105 4 VAL B CA 1654 C C . VAL B 5 ? 0.4016 0.3874 0.3612 0.0205 0.0164 -0.0098 4 VAL B C 1655 O O . VAL B 5 ? 0.4485 0.4430 0.4126 0.0186 0.0196 -0.0124 4 VAL B O 1656 C CB . VAL B 5 ? 0.4300 0.4068 0.3889 0.0205 0.0108 -0.0097 4 VAL B CB 1657 C CG1 . VAL B 5 ? 0.3891 0.3551 0.3455 0.0228 0.0084 -0.0101 4 VAL B CG1 1658 C CG2 . VAL B 5 ? 0.4138 0.4030 0.3798 0.0164 0.0125 -0.0123 4 VAL B CG2 1659 N N . GLU B 6 ? 0.4199 0.4051 0.3764 0.0205 0.0146 -0.0061 5 GLU B N 1660 C CA . GLU B 6 ? 0.3938 0.3897 0.3527 0.0178 0.0162 -0.0051 5 GLU B CA 1661 C C . GLU B 6 ? 0.4181 0.4239 0.3818 0.0136 0.0148 -0.0053 5 GLU B C 1662 O O . GLU B 6 ? 0.3837 0.3864 0.3463 0.0132 0.0113 -0.0036 5 GLU B O 1663 C CB . GLU B 6 ? 0.4302 0.4222 0.3842 0.0194 0.0150 -0.0010 5 GLU B CB 1664 C CG . GLU B 6 ? 0.4726 0.4754 0.4290 0.0169 0.0168 0.0001 5 GLU B CG 1665 C CD . GLU B 6 ? 0.6373 0.6436 0.5951 0.0175 0.0211 -0.0020 5 GLU B CD 1666 O OE1 . GLU B 6 ? 0.6015 0.5996 0.5567 0.0208 0.0224 -0.0032 5 GLU B OE1 1667 O OE2 . GLU B 6 ? 0.5741 0.5912 0.5354 0.0148 0.0231 -0.0023 5 GLU B OE2 1668 N N . PRO B 7 ? 0.4438 0.4612 0.4128 0.0105 0.0174 -0.0074 6 PRO B N 1669 C CA . PRO B 7 ? 0.3840 0.4103 0.3577 0.0065 0.0160 -0.0078 6 PRO B CA 1670 C C . PRO B 7 ? 0.3951 0.4245 0.3677 0.0049 0.0135 -0.0041 6 PRO B C 1671 O O . PRO B 7 ? 0.4468 0.4779 0.4209 0.0030 0.0108 -0.0035 6 PRO B O 1672 C CB . PRO B 7 ? 0.4845 0.5222 0.4639 0.0037 0.0199 -0.0109 6 PRO B CB 1673 C CG . PRO B 7 ? 0.4235 0.4562 0.4014 0.0067 0.0229 -0.0130 6 PRO B CG 1674 C CD . PRO B 7 ? 0.4326 0.4551 0.4041 0.0104 0.0216 -0.0099 6 PRO B CD 1675 N N . HIS B 8 ? 0.4422 0.4723 0.4122 0.0057 0.0142 -0.0016 7 HIS B N 1676 C CA . HIS B 8 ? 0.3206 0.3542 0.2897 0.0042 0.0120 0.0019 7 HIS B CA 1677 C C . HIS B 8 ? 0.4420 0.4675 0.4051 0.0073 0.0113 0.0054 7 HIS B C 1678 O O . HIS B 8 ? 0.4552 0.4782 0.4164 0.0094 0.0138 0.0051 7 HIS B O 1679 C CB . HIS B 8 ? 0.3286 0.3759 0.3025 0.0004 0.0139 0.0016 7 HIS B CB 1680 C CG . HIS B 8 ? 0.4427 0.4983 0.4225 -0.0032 0.0140 -0.0012 7 HIS B CG 1681 N ND1 . HIS B 8 ? 0.5393 0.5971 0.5225 -0.0037 0.0165 -0.0052 7 HIS B ND1 1682 C CD2 . HIS B 8 ? 0.5471 0.6090 0.5299 -0.0063 0.0120 -0.0006 7 HIS B CD2 1683 C CE1 . HIS B 8 ? 0.5882 0.6534 0.5763 -0.0070 0.0161 -0.0069 7 HIS B CE1 1684 N NE2 . HIS B 8 ? 0.6040 0.6718 0.5919 -0.0087 0.0133 -0.0042 7 HIS B NE2 1685 N N . VAL B 9 ? 0.4543 0.4755 0.4143 0.0077 0.0079 0.0087 8 VAL B N 1686 C CA . VAL B 9 ? 0.3849 0.3965 0.3386 0.0110 0.0067 0.0121 8 VAL B CA 1687 C C . VAL B 9 ? 0.4170 0.4316 0.3698 0.0095 0.0043 0.0159 8 VAL B C 1688 O O . VAL B 9 ? 0.3968 0.4159 0.3522 0.0070 0.0022 0.0160 8 VAL B O 1689 C CB . VAL B 9 ? 0.4246 0.4230 0.3742 0.0143 0.0049 0.0117 8 VAL B CB 1690 C CG1 . VAL B 9 ? 0.4335 0.4223 0.3771 0.0167 0.0022 0.0156 8 VAL B CG1 1691 C CG2 . VAL B 9 ? 0.3894 0.3833 0.3382 0.0168 0.0078 0.0091 8 VAL B CG2 1692 N N . THR B 10 ? 0.3640 0.3765 0.3132 0.0110 0.0049 0.0189 9 THR B N 1693 C CA . THR B 10 ? 0.4373 0.4506 0.3847 0.0103 0.0025 0.0229 9 THR B CA 1694 C C . THR B 10 ? 0.3893 0.3892 0.3302 0.0138 0.0002 0.0255 9 THR B C 1695 O O . THR B 10 ? 0.3592 0.3499 0.2965 0.0170 0.0011 0.0249 9 THR B O 1696 C CB . THR B 10 ? 0.3960 0.4172 0.3441 0.0091 0.0046 0.0250 9 THR B CB 1697 O OG1 . THR B 10 ? 0.5551 0.5722 0.5008 0.0117 0.0074 0.0248 9 THR B OG1 1698 C CG2 . THR B 10 ? 0.3058 0.3409 0.2603 0.0051 0.0062 0.0230 9 THR B CG2 1699 N N . ALA B 11 ? 0.4278 0.4265 0.3671 0.0131 -0.0028 0.0284 10 ALA B N 1700 C CA . ALA B 11 ? 0.3718 0.3590 0.3092 0.0142 -0.0055 0.0294 10 ALA B CA 1701 C C . ALA B 11 ? 0.3676 0.3568 0.3066 0.0116 -0.0070 0.0315 10 ALA B C 1702 O O . ALA B 11 ? 0.3216 0.3171 0.2619 0.0096 -0.0079 0.0321 10 ALA B O 1703 C CB . ALA B 11 ? 0.3683 0.3502 0.3047 0.0148 -0.0083 0.0288 10 ALA B CB 1704 N N . VAL B 12 ? 0.3328 0.3170 0.2722 0.0119 -0.0071 0.0322 11 VAL B N 1705 C CA . VAL B 12 ? 0.3728 0.3577 0.3129 0.0097 -0.0084 0.0338 11 VAL B CA 1706 C C . VAL B 12 ? 0.3832 0.3648 0.3248 0.0086 -0.0117 0.0352 11 VAL B C 1707 O O . VAL B 12 ? 0.3794 0.3571 0.3230 0.0106 -0.0117 0.0350 11 VAL B O 1708 C CB . VAL B 12 ? 0.3465 0.3299 0.2872 0.0102 -0.0068 0.0340 11 VAL B CB 1709 C CG1 . VAL B 12 ? 0.2884 0.2715 0.2289 0.0081 -0.0082 0.0353 11 VAL B CG1 1710 C CG2 . VAL B 12 ? 0.3109 0.2995 0.2515 0.0110 -0.0033 0.0330 11 VAL B CG2 1711 N N . TRP B 13 ? 0.3042 0.2863 0.2444 0.0066 -0.0134 0.0353 12 TRP B N 1712 C CA . TRP B 13 ? 0.2626 0.2442 0.2063 0.0052 -0.0159 0.0361 12 TRP B CA 1713 C C . TRP B 13 ? 0.3122 0.2943 0.2610 0.0064 -0.0150 0.0380 12 TRP B C 1714 O O . TRP B 13 ? 0.4156 0.3961 0.3635 0.0057 -0.0146 0.0380 12 TRP B O 1715 C CB . TRP B 13 ? 0.2913 0.2688 0.2284 0.0071 -0.0156 0.0341 12 TRP B CB 1716 C CG . TRP B 13 ? 0.3237 0.2974 0.2594 0.0097 -0.0164 0.0330 12 TRP B CG 1717 C CD1 . TRP B 13 ? 0.3119 0.2920 0.2497 0.0113 -0.0166 0.0336 12 TRP B CD1 1718 C CD2 . TRP B 13 ? 0.3594 0.3265 0.2932 0.0123 -0.0158 0.0316 12 TRP B CD2 1719 N NE1 . TRP B 13 ? 0.3026 0.2837 0.2424 0.0139 -0.0161 0.0341 12 TRP B NE1 1720 C CE2 . TRP B 13 ? 0.2889 0.2703 0.2307 0.0168 -0.0129 0.0347 12 TRP B CE2 1721 C CE3 . TRP B 13 ? 0.3606 0.3443 0.3118 0.0019 -0.0188 0.0398 12 TRP B CE3 1722 C CZ2 . TRP B 13 ? 0.2854 0.2721 0.2329 0.0164 -0.0128 0.0382 12 TRP B CZ2 1723 C CZ3 . TRP B 13 ? 0.3147 0.3065 0.2716 0.0076 -0.0149 0.0432 12 TRP B CZ3 1724 C CH2 . TRP B 13 ? 0.2845 0.2749 0.2376 0.0139 -0.0126 0.0418 12 TRP B CH2 1725 N N . GLY B 14 ? 0.3117 0.2919 0.2624 0.0090 -0.0148 0.0385 13 GLY B N 1726 C CA . GLY B 14 ? 0.3015 0.2750 0.2506 0.0113 -0.0145 0.0387 13 GLY B CA 1727 C C . GLY B 14 ? 0.4028 0.3696 0.3493 0.0134 -0.0128 0.0364 13 GLY B C 1728 O O . GLY B 14 ? 0.3252 0.2860 0.2696 0.0152 -0.0123 0.0357 13 GLY B O 1729 N N . LYS B 15 ? 0.3806 0.3486 0.3270 0.0134 -0.0119 0.0351 14 LYS B N 1730 C CA . LYS B 15 ? 0.4229 0.3849 0.3671 0.0158 -0.0100 0.0327 14 LYS B CA 1731 C C . LYS B 15 ? 0.4063 0.3651 0.3500 0.0170 -0.0100 0.0304 14 LYS B C 1732 O O . LYS B 15 ? 0.4943 0.4533 0.4388 0.0165 -0.0115 0.0304 14 LYS B O 1733 C CB . LYS B 15 ? 0.3709 0.3365 0.3152 0.0152 -0.0084 0.0330 14 LYS B CB 1734 C CG . LYS B 15 ? 0.3627 0.3296 0.3068 0.0144 -0.0084 0.0348 14 LYS B CG 1735 C CD . LYS B 15 ? 0.4917 0.4625 0.4356 0.0135 -0.0068 0.0349 14 LYS B CD 1736 C CE . LYS B 15 ? 0.5610 0.5320 0.5044 0.0133 -0.0064 0.0362 14 LYS B CE 1737 N NZ . LYS B 15 ? 0.5612 0.5258 0.5034 0.0163 -0.0052 0.0354 14 LYS B NZ 1738 N N . ASN B 16 ? 0.4469 0.4028 0.3893 0.0186 -0.0082 0.0283 15 ASN B N 1739 C CA . ASN B 16 ? 0.4496 0.4004 0.3897 0.0205 -0.0077 0.0255 15 ASN B CA 1740 C C . ASN B 16 ? 0.5082 0.4610 0.4460 0.0213 -0.0064 0.0249 15 ASN B C 1741 O O . ASN B 16 ? 0.4887 0.4463 0.4266 0.0208 -0.0050 0.0261 15 ASN B O 1742 C CB . ASN B 16 ? 0.3404 0.2850 0.2787 0.0225 -0.0062 0.0230 15 ASN B CB 1743 C CG . ASN B 16 ? 0.5708 0.5110 0.5067 0.0232 -0.0066 0.0231 15 ASN B CG 1744 O OD1 . ASN B 16 ? 0.5840 0.5242 0.5203 0.0223 -0.0083 0.0244 15 ASN B OD1 1745 N ND2 . ASN B 16 ? 0.6829 0.6194 0.6162 0.0249 -0.0048 0.0218 15 ASN B ND2 1746 N N . VAL B 17 ? 0.4138 0.3632 0.3498 0.0225 -0.0065 0.0230 16 VAL B N 1747 C CA . VAL B 17 ? 0.3901 0.3406 0.3237 0.0239 -0.0047 0.0219 16 VAL B CA 1748 C C . VAL B 17 ? 0.4544 0.3981 0.3862 0.0259 -0.0045 0.0190 16 VAL B C 1749 O O . VAL B 17 ? 0.4473 0.3875 0.3797 0.0255 -0.0065 0.0181 16 VAL B O 1750 C CB . VAL B 17 ? 0.4518 0.4093 0.3848 0.0223 -0.0056 0.0233 16 VAL B CB 1751 C CG1 . VAL B 17 ? 0.4352 0.3907 0.3681 0.0216 -0.0084 0.0229 16 VAL B CG1 1752 C CG2 . VAL B 17 ? 0.3587 0.3200 0.2896 0.0234 -0.0027 0.0222 16 VAL B CG2 1753 N N . SER B 18 ? 0.3963 0.3389 0.3263 0.0278 -0.0020 0.0174 17 SER B N 1754 C CA . SER B 18 ? 0.4014 0.3383 0.3300 0.0297 -0.0014 0.0145 17 SER B CA 1755 C C . SER B 18 ? 0.4672 0.4054 0.3940 0.0304 -0.0013 0.0142 17 SER B C 1756 O O . SER B 18 ? 0.4876 0.4337 0.4156 0.0295 0.0009 0.0141 17 SER B O 1757 C CB . SER B 18 ? 0.3338 0.2686 0.2616 0.0314 0.0016 0.0127 17 SER B CB 1758 O OG . SER B 18 ? 0.5118 0.4425 0.4388 0.0325 0.0022 0.0099 17 SER B OG 1759 N N . LEU B 19 ? 0.3451 0.2795 0.2721 0.0304 -0.0033 0.0127 18 LEU B N 1760 C CA . LEU B 19 ? 0.3427 0.2823 0.2730 0.0291 -0.0029 0.0103 18 LEU B CA 1761 C C . LEU B 19 ? 0.3794 0.3136 0.3095 0.0315 -0.0008 0.0071 18 LEU B C 1762 O O . LEU B 19 ? 0.4237 0.3499 0.3521 0.0330 -0.0024 0.0063 18 LEU B O 1763 C CB . LEU B 19 ? 0.4116 0.3516 0.3433 0.0272 -0.0064 0.0106 18 LEU B CB 1764 C CG . LEU B 19 ? 0.3806 0.3267 0.3131 0.0246 -0.0085 0.0135 18 LEU B CG 1765 C CD1 . LEU B 19 ? 0.3399 0.2894 0.2758 0.0220 -0.0110 0.0126 18 LEU B CD1 1766 C CD2 . LEU B 19 ? 0.5264 0.4843 0.4626 0.0222 -0.0057 0.0134 18 LEU B CD2 1767 N N . LYS B 20 ? 0.3797 0.3197 0.3126 0.0313 0.0029 0.0050 19 LYS B N 1768 C CA . LYS B 20 ? 0.4319 0.3669 0.3643 0.0338 0.0054 0.0023 19 LYS B CA 1769 C C . LYS B 20 ? 0.3852 0.3236 0.3224 0.0324 0.0057 -0.0014 19 LYS B C 1770 O O . LYS B 20 ? 0.4397 0.3885 0.3823 0.0288 0.0060 -0.0027 19 LYS B O 1771 C CB . LYS B 20 ? 0.4360 0.3765 0.3696 0.0341 0.0093 0.0016 19 LYS B CB 1772 C CG . LYS B 20 ? 0.5112 0.4503 0.4464 0.0355 0.0122 -0.0016 19 LYS B CG 1773 C CD . LYS B 20 ? 0.5914 0.5393 0.5298 0.0345 0.0161 -0.0029 19 LYS B CD 1774 C CE . LYS B 20 ? 0.7119 0.6635 0.6571 0.0323 0.0170 -0.0048 19 LYS B CE 1775 N NZ . LYS B 20 ? 0.7636 0.7237 0.7132 0.0307 0.0198 -0.0058 19 LYS B NZ 1776 N N . CYS B 21 ? 0.3728 0.3045 0.3094 0.0339 0.0054 -0.0028 20 CYS B N 1777 C CA . CYS B 21 ? 0.3914 0.3264 0.3330 0.0325 0.0060 -0.0061 20 CYS B CA 1778 C C . CYS B 21 ? 0.3692 0.3054 0.3147 0.0311 0.0063 -0.0063 20 CYS B C 1779 O O . CYS B 21 ? 0.4085 0.3414 0.3527 0.0306 0.0041 -0.0045 20 CYS B O 1780 C CB . CYS B 21 ? 0.4103 0.3418 0.3512 0.0322 0.0027 -0.0061 20 CYS B CB 1781 S SG . CYS B 21 ? 0.4411 0.3777 0.3883 0.0302 0.0036 -0.0103 20 CYS B SG 1782 N N . LEU B 22 ? 0.4105 0.3526 0.3614 0.0300 0.0091 -0.0086 21 LEU B N 1783 C CA . LEU B 22 ? 0.5104 0.4542 0.4659 0.0286 0.0093 -0.0091 21 LEU B CA 1784 C C . LEU B 22 ? 0.5341 0.4817 0.4954 0.0271 0.0099 -0.0122 21 LEU B C 1785 O O . LEU B 22 ? 0.5196 0.4723 0.4837 0.0264 0.0119 -0.0149 21 LEU B O 1786 C CB . LEU B 22 ? 0.4485 0.3961 0.4061 0.0282 0.0115 -0.0093 21 LEU B CB 1787 C CG . LEU B 22 ? 0.5224 0.4671 0.4744 0.0296 0.0115 -0.0065 21 LEU B CG 1788 C CD1 . LEU B 22 ? 0.5442 0.4938 0.4990 0.0291 0.0140 -0.0071 21 LEU B CD1 1789 C CD2 . LEU B 22 ? 0.4704 0.4106 0.4193 0.0297 0.0093 -0.0042 21 LEU B CD2 1790 N N . ILE B 23 ? 0.5162 0.4625 0.4799 0.0264 0.0084 -0.0120 22 ILE B N 1791 C CA . ILE B 23 ? 0.6130 0.5618 0.5818 0.0251 0.0086 -0.0145 22 ILE B CA 1792 C C . ILE B 23 ? 0.5254 0.4767 0.4978 0.0245 0.0098 -0.0156 22 ILE B C 1793 O O . ILE B 23 ? 0.4271 0.3738 0.3958 0.0256 0.0088 -0.0137 22 ILE B O 1794 C CB . ILE B 23 ? 0.5452 0.4891 0.5118 0.0254 0.0058 -0.0132 22 ILE B CB 1795 C CG1 . ILE B 23 ? 0.3666 0.3059 0.3268 0.0267 0.0039 -0.0115 22 ILE B CG1 1796 C CG2 . ILE B 23 ? 0.5397 0.4859 0.5110 0.0242 0.0061 -0.0157 22 ILE B CG2 1797 C CD1 . ILE B 23 ? 0.3561 0.2910 0.3139 0.0267 0.0008 -0.0096 22 ILE B CD1 1798 N N . GLU B 24 ? 0.5496 0.5072 0.5271 0.0233 0.0120 -0.0185 23 GLU B N 1799 C CA . GLU B 24 ? 0.7177 0.6765 0.6968 0.0233 0.0132 -0.0193 23 GLU B CA 1800 C C . GLU B 24 ? 0.7027 0.6658 0.6875 0.0221 0.0137 -0.0225 23 GLU B C 1801 O O . GLU B 24 ? 0.6933 0.6625 0.6819 0.0213 0.0150 -0.0250 23 GLU B O 1802 C CB . GLU B 24 ? 0.6880 0.6506 0.6678 0.0232 0.0151 -0.0197 23 GLU B CB 1803 C CG . GLU B 24 ? 0.7358 0.6942 0.7100 0.0245 0.0146 -0.0165 23 GLU B CG 1804 C CD . GLU B 24 ? 0.8270 0.7887 0.8018 0.0243 0.0165 -0.0167 23 GLU B CD 1805 O OE1 . GLU B 24 ? 0.6696 0.6383 0.6492 0.0229 0.0180 -0.0195 23 GLU B OE1 1806 O OE2 . GLU B 24 ? 1.0279 0.9856 0.9981 0.0256 0.0164 -0.0140 23 GLU B OE2 1807 N N . VAL B 25 ? 0.7238 0.6837 0.7086 0.0220 0.0122 -0.0222 24 VAL B N 1808 C CA . VAL B 25 ? 0.7666 0.7304 0.7567 0.0208 0.0125 -0.0251 24 VAL B CA 1809 C C . VAL B 25 ? 0.8387 0.8017 0.8298 0.0213 0.0127 -0.0255 24 VAL B C 1810 O O . VAL B 25 ? 0.8282 0.7960 0.8231 0.0207 0.0125 -0.0277 24 VAL B O 1811 C CB . VAL B 25 ? 0.6106 0.5715 0.6008 0.0203 0.0111 -0.0247 24 VAL B CB 1812 C CG1 . VAL B 25 ? 0.4875 0.4490 0.4759 0.0201 0.0112 -0.0248 24 VAL B CG1 1813 C CG2 . VAL B 25 ? 0.5607 0.5141 0.5455 0.0218 0.0091 -0.0213 24 VAL B CG2 1814 N N . ASN B 26 ? 0.8106 0.7683 0.7973 0.0226 0.0123 -0.0227 25 ASN B N 1815 C CA . ASN B 26 ? 0.8262 0.7829 0.8134 0.0230 0.0126 -0.0228 25 ASN B CA 1816 C C . ASN B 26 ? 0.7452 0.7010 0.7347 0.0226 0.0117 -0.0237 25 ASN B C 1817 O O . ASN B 26 ? 0.7718 0.7295 0.7642 0.0224 0.0120 -0.0252 25 ASN B O 1818 C CB . ASN B 26 ? 0.8304 0.7925 0.8208 0.0226 0.0141 -0.0250 25 ASN B CB 1819 C CG . ASN B 26 ? 1.0050 0.9670 0.9927 0.0231 0.0152 -0.0237 25 ASN B CG 1820 O OD1 . ASN B 26 ? 0.9997 0.9567 0.9825 0.0240 0.0147 -0.0208 25 ASN B OD1 1821 N ND2 . ASN B 26 ? 1.0559 1.0235 1.0461 0.0227 0.0163 -0.0255 25 ASN B ND2 1822 N N . GLU B 27 ? 0.7310 0.6837 0.7186 0.0225 0.0103 -0.0224 26 GLU B N 1823 C CA . GLU B 27 ? 0.5970 0.5486 0.5864 0.0219 0.0093 -0.0229 26 GLU B CA 1824 C C . GLU B 27 ? 0.6054 0.5505 0.5884 0.0232 0.0070 -0.0197 26 GLU B C 1825 O O . GLU B 27 ? 0.7086 0.6509 0.6865 0.0242 0.0061 -0.0175 26 GLU B O 1826 C CB . GLU B 27 ? 0.5938 0.5492 0.5872 0.0204 0.0098 -0.0249 26 GLU B CB 1827 C CG . GLU B 27 ? 0.7048 0.6585 0.6996 0.0196 0.0091 -0.0249 26 GLU B CG 1828 C CD . GLU B 27 ? 0.8227 0.7830 0.8227 0.0173 0.0104 -0.0271 26 GLU B CD 1829 O OE1 . GLU B 27 ? 0.9436 0.9112 0.9461 0.0174 0.0095 -0.0293 26 GLU B OE1 1830 O OE2 . GLU B 27 ? 0.8147 0.7731 0.8148 0.0162 0.0107 -0.0265 26 GLU B OE2 1831 N N . THR B 28 ? 0.6248 0.5676 0.6079 0.0231 0.0058 -0.0194 27 THR B N 1832 C CA . THR B 28 ? 0.5485 0.4859 0.5255 0.0241 0.0030 -0.0167 27 THR B CA 1833 C C . THR B 28 ? 0.5434 0.4802 0.5192 0.0238 0.0016 -0.0160 27 THR B C 1834 O O . THR B 28 ? 0.5020 0.4412 0.4820 0.0225 0.0020 -0.0173 27 THR B O 1835 C CB . THR B 28 ? 0.5836 0.5191 0.5609 0.0241 0.0020 -0.0167 27 THR B CB 1836 O OG1 . THR B 28 ? 0.6086 0.5457 0.5888 0.0241 0.0037 -0.0180 27 THR B OG1 1837 C CG2 . THR B 28 ? 0.5403 0.4705 0.5105 0.0254 -0.0008 -0.0143 27 THR B CG2 1838 N N . ILE B 29 ? 0.5071 0.4407 0.4771 0.0248 0.0000 -0.0138 28 ILE B N 1839 C CA . ILE B 29 ? 0.4935 0.4263 0.4620 0.0245 -0.0014 -0.0128 28 ILE B CA 1840 C C . ILE B 29 ? 0.3827 0.3119 0.3482 0.0246 -0.0044 -0.0115 28 ILE B C 1841 O O . ILE B 29 ? 0.4473 0.3728 0.4077 0.0255 -0.0059 -0.0102 28 ILE B O 1842 C CB . ILE B 29 ? 0.5832 0.5148 0.5472 0.0254 -0.0016 -0.0113 28 ILE B CB 1843 C CG1 . ILE B 29 ? 0.4997 0.4353 0.4669 0.0252 0.0013 -0.0126 28 ILE B CG1 1844 C CG2 . ILE B 29 ? 0.4692 0.3998 0.4316 0.0251 -0.0033 -0.0101 28 ILE B CG2 1845 C CD1 . ILE B 29 ? 0.4964 0.4366 0.4692 0.0238 0.0026 -0.0147 28 ILE B CD1 1846 N N . THR B 30 ? 0.4573 0.3877 0.4260 0.0234 -0.0050 -0.0121 29 THR B N 1847 C CA . THR B 30 ? 0.3789 0.3061 0.3450 0.0233 -0.0080 -0.0108 29 THR B CA 1848 C C . THR B 30 ? 0.4595 0.3842 0.4208 0.0236 -0.0102 -0.0089 29 THR B C 1849 O O . THR B 30 ? 0.5033 0.4244 0.4592 0.0243 -0.0123 -0.0075 29 THR B O 1850 C CB . THR B 30 ? 0.4293 0.3587 0.4005 0.0219 -0.0078 -0.0121 29 THR B CB 1851 O OG1 . THR B 30 ? 0.5138 0.4452 0.4890 0.0216 -0.0057 -0.0139 29 THR B OG1 1852 C CG2 . THR B 30 ? 0.4301 0.3564 0.3987 0.0217 -0.0110 -0.0108 29 THR B CG2 1853 N N . GLN B 31 ? 0.4214 0.3482 0.3847 0.0231 -0.0095 -0.0089 30 GLN B N 1854 C CA . GLN B 31 ? 0.3084 0.2333 0.2675 0.0233 -0.0111 -0.0071 30 GLN B CA 1855 C C . GLN B 31 ? 0.4205 0.3459 0.3788 0.0239 -0.0103 -0.0077 30 GLN B C 1856 O O . GLN B 31 ? 0.4485 0.3760 0.4098 0.0238 -0.0088 -0.0099 30 GLN B O 1857 C CB . GLN B 31 ? 0.3222 0.2446 0.2792 0.0228 -0.0144 -0.0059 30 GLN B CB 1858 C CG . GLN B 31 ? 0.2840 0.2054 0.2408 0.0226 -0.0162 -0.0066 30 GLN B CG 1859 C CD . GLN B 31 ? 0.4048 0.3240 0.3600 0.0218 -0.0197 -0.0054 30 GLN B CD 1860 O OE1 . GLN B 31 ? 0.4273 0.3461 0.3822 0.0214 -0.0202 -0.0046 30 GLN B OE1 1861 N NE2 . GLN B 31 ? 0.4079 0.3258 0.3622 0.0214 -0.0221 -0.0054 30 GLN B NE2 1862 N N . ILE B 32 ? 0.3912 0.3150 0.3452 0.0245 -0.0111 -0.0061 31 ILE B N 1863 C CA . ILE B 32 ? 0.4044 0.3281 0.3565 0.0254 -0.0104 -0.0063 31 ILE B CA 1864 C C . ILE B 32 ? 0.3769 0.2975 0.3246 0.0254 -0.0134 -0.0044 31 ILE B C 1865 O O . ILE B 32 ? 0.3976 0.3169 0.3436 0.0248 -0.0152 -0.0027 31 ILE B O 1866 C CB . ILE B 32 ? 0.3439 0.2694 0.2957 0.0260 -0.0077 -0.0060 31 ILE B CB 1867 C CG1 . ILE B 32 ? 0.3936 0.3176 0.3423 0.0259 -0.0087 -0.0039 31 ILE B CG1 1868 C CG2 . ILE B 32 ? 0.3493 0.2782 0.3061 0.0255 -0.0053 -0.0076 31 ILE B CG2 1869 C CD1 . ILE B 32 ? 0.3653 0.2905 0.3134 0.0265 -0.0065 -0.0038 31 ILE B CD1 1870 N N . SER B 33 ? 0.4252 0.3453 0.3716 0.0260 -0.0138 -0.0047 32 SER B N 1871 C CA . SER B 33 ? 0.3641 0.2821 0.3074 0.0257 -0.0170 -0.0024 32 SER B CA 1872 C C . SER B 33 ? 0.4691 0.3880 0.4109 0.0265 -0.0164 -0.0020 32 SER B C 1873 O O . SER B 33 ? 0.3972 0.3245 0.3438 0.0250 -0.0131 -0.0046 32 SER B O 1874 C CB . SER B 33 ? 0.3477 0.2645 0.2924 0.0244 -0.0202 -0.0025 32 SER B CB 1875 O OG . SER B 33 ? 0.4765 0.3981 0.4249 0.0232 -0.0196 -0.0045 32 SER B OG 1876 N N . TRP B 34 ? 0.3975 0.3165 0.3364 0.0260 -0.0183 0.0013 33 TRP B N 1877 C CA . TRP B 34 ? 0.3447 0.2747 0.2868 0.0230 -0.0175 0.0022 33 TRP B CA 1878 C C . TRP B 34 ? 0.3930 0.3272 0.3375 0.0202 -0.0206 0.0033 33 TRP B C 1879 O O . TRP B 34 ? 0.4250 0.3518 0.3659 0.0211 -0.0242 0.0054 33 TRP B O 1880 C CB . TRP B 34 ? 0.3221 0.2496 0.2595 0.0245 -0.0173 0.0052 33 TRP B CB 1881 C CG . TRP B 34 ? 0.3474 0.2752 0.2841 0.0263 -0.0135 0.0042 33 TRP B CG 1882 C CD1 . TRP B 34 ? 0.2962 0.2169 0.2294 0.0289 -0.0122 0.0041 33 TRP B CD1 1883 C CD2 . TRP B 34 ? 0.3003 0.2389 0.2413 0.0244 -0.0100 0.0026 33 TRP B CD2 1884 N NE1 . TRP B 34 ? 0.3002 0.2220 0.2328 0.0306 -0.0089 0.0033 33 TRP B NE1 1885 C CE2 . TRP B 34 ? 0.3048 0.2393 0.2432 0.0272 -0.0072 0.0021 33 TRP B CE2 1886 C CE3 . TRP B 34 ? 0.3296 0.2810 0.2766 0.0206 -0.0089 0.0016 33 TRP B CE3 1887 C CZ2 . TRP B 34 ? 0.3845 0.3272 0.3259 0.0262 -0.0035 0.0007 33 TRP B CZ2 1888 C CZ3 . TRP B 34 ? 0.3425 0.3020 0.2925 0.0196 -0.0052 0.0001 33 TRP B CZ3 1889 C CH2 . TRP B 34 ? 0.3666 0.3217 0.3137 0.0224 -0.0025 -0.0003 33 TRP B CH2 1890 N N . GLU B 35 ? 0.4091 0.3553 0.3596 0.0167 -0.0194 0.0021 34 GLU B N 1891 C CA . GLU B 35 ? 0.5131 0.4646 0.4664 0.0136 -0.0221 0.0031 34 GLU B CA 1892 C C . GLU B 35 ? 0.3821 0.3447 0.3384 0.0108 -0.0210 0.0040 34 GLU B C 1893 O O . GLU B 35 ? 0.3957 0.3636 0.3532 0.0107 -0.0177 0.0031 34 GLU B O 1894 C CB . GLU B 35 ? 0.4866 0.4415 0.4452 0.0118 -0.0222 0.0002 34 GLU B CB 1895 C CG . GLU B 35 ? 0.4973 0.4415 0.4533 0.0144 -0.0233 -0.0008 34 GLU B CG 1896 C CD . GLU B 35 ? 0.6026 0.5503 0.5639 0.0128 -0.0228 -0.0038 34 GLU B CD 1897 O OE1 . GLU B 35 ? 0.6135 0.5720 0.5806 0.0096 -0.0213 -0.0053 34 GLU B OE1 1898 O OE2 . GLU B 35 ? 0.7283 0.6679 0.6881 0.0147 -0.0238 -0.0047 34 GLU B OE2 1899 N N . LYS B 36 ? 0.4875 0.4537 0.4449 0.0086 -0.0237 0.0059 35 LYS B N 1900 C CA . LYS B 36 ? 0.4959 0.4727 0.4561 0.0058 -0.0231 0.0070 35 LYS B CA 1901 C C . LYS B 36 ? 0.5709 0.5568 0.5373 0.0021 -0.0238 0.0056 35 LYS B C 1902 O O . LYS B 36 ? 0.6591 0.6415 0.6257 0.0017 -0.0267 0.0059 35 LYS B O 1903 C CB . LYS B 36 ? 0.5168 0.4901 0.4725 0.0065 -0.0256 0.0110 35 LYS B CB 1904 C CG . LYS B 36 ? 0.5113 0.4951 0.4693 0.0040 -0.0247 0.0125 35 LYS B CG 1905 C CD . LYS B 36 ? 0.4697 0.4488 0.4224 0.0057 -0.0260 0.0163 35 LYS B CD 1906 C CE . LYS B 36 ? 0.4879 0.4773 0.4427 0.0034 -0.0246 0.0177 35 LYS B CE 1907 N NZ . LYS B 36 ? 0.6184 0.6165 0.5778 -0.0001 -0.0263 0.0180 35 LYS B NZ 1908 N N . ILE B 37 ? 0.5588 0.5562 0.5302 -0.0007 -0.0211 0.0042 36 ILE B N 1909 C CA . ILE B 37 ? 0.6196 0.6263 0.5970 -0.0044 -0.0215 0.0028 36 ILE B CA 1910 C C . ILE B 37 ? 0.6777 0.6865 0.6546 -0.0060 -0.0247 0.0058 36 ILE B C 1911 O O . ILE B 37 ? 0.6675 0.6775 0.6419 -0.0057 -0.0250 0.0084 36 ILE B O 1912 C CB . ILE B 37 ? 0.5429 0.5612 0.5255 -0.0069 -0.0176 0.0004 36 ILE B CB 1913 C CG1 . ILE B 37 ? 0.5383 0.5563 0.5236 -0.0065 -0.0149 -0.0033 36 ILE B CG1 1914 C CG2 . ILE B 37 ? 0.4613 0.4904 0.4492 -0.0109 -0.0181 0.0003 36 ILE B CG2 1915 C CD1 . ILE B 37 ? 0.5318 0.5410 0.5128 -0.0028 -0.0135 -0.0037 36 ILE B CD1 1916 N N . HIS B 38 ? 0.7550 0.7645 0.7345 -0.0076 -0.0272 0.0054 37 HIS B N 1917 C CA . HIS B 38 ? 0.7631 0.7755 0.7431 -0.0095 -0.0303 0.0079 37 HIS B CA 1918 C C . HIS B 38 ? 0.8103 0.8305 0.7966 -0.0128 -0.0305 0.0058 37 HIS B C 1919 O O . HIS B 38 ? 0.9394 0.9551 0.9265 -0.0127 -0.0323 0.0049 37 HIS B O 1920 C CB . HIS B 38 ? 0.7751 0.7764 0.7497 -0.0071 -0.0341 0.0105 37 HIS B CB 1921 C CG . HIS B 38 ? 0.7694 0.7635 0.7377 -0.0041 -0.0342 0.0130 37 HIS B CG 1922 N ND1 . HIS B 38 ? 0.6843 0.6661 0.6470 -0.0008 -0.0358 0.0139 37 HIS B ND1 1923 C CD2 . HIS B 38 ? 0.7910 0.7885 0.7576 -0.0040 -0.0328 0.0148 37 HIS B CD2 1924 C CE1 . HIS B 38 ? 0.7327 0.7104 0.6906 0.0013 -0.0354 0.0162 37 HIS B CE1 1925 N NE2 . HIS B 38 ? 0.8280 0.8151 0.7882 -0.0006 -0.0336 0.0168 37 HIS B NE2 1926 N N . GLY B 39 ? 0.8495 0.8812 0.8404 -0.0159 -0.0286 0.0051 38 GLY B N 1927 C CA . GLY B 39 ? 0.8467 0.8863 0.8440 -0.0191 -0.0280 0.0027 38 GLY B CA 1928 C C . GLY B 39 ? 0.8513 0.8901 0.8508 -0.0186 -0.0252 -0.0007 38 GLY B C 1929 O O . GLY B 39 ? 0.8659 0.9052 0.8646 -0.0175 -0.0221 -0.0019 38 GLY B O 1930 N N . LYS B 40 ? 0.8496 0.8867 0.8517 -0.0193 -0.0262 -0.0024 39 LYS B N 1931 C CA . LYS B 40 ? 0.9824 1.0165 0.9857 -0.0182 -0.0239 -0.0054 39 LYS B CA 1932 C C . LYS B 40 ? 0.9992 1.0203 0.9970 -0.0143 -0.0256 -0.0046 39 LYS B C 1933 O O . LYS B 40 ? 1.0740 1.0911 1.0706 -0.0123 -0.0233 -0.0064 39 LYS B O 1934 C CB . LYS B 40 ? 1.0080 1.0474 1.0174 -0.0210 -0.0236 -0.0078 39 LYS B CB 1935 C CG . LYS B 40 ? 1.0307 1.0681 1.0423 -0.0202 -0.0211 -0.0111 39 LYS B CG 1936 C CD . LYS B 40 ? 1.0655 1.1008 1.0750 -0.0180 -0.0176 -0.0125 39 LYS B CD 1937 C CE . LYS B 40 ? 0.9613 1.0071 0.9742 -0.0201 -0.0137 -0.0141 39 LYS B CE 1938 N NZ . LYS B 40 ? 0.9339 0.9761 0.9431 -0.0174 -0.0112 -0.0144 39 LYS B NZ 1939 N N . SER B 41 ? 0.9034 0.9177 0.8977 -0.0132 -0.0296 -0.0020 40 SER B N 1940 C CA . SER B 41 ? 0.8587 0.8605 0.8474 -0.0095 -0.0312 -0.0011 40 SER B CA 1941 C C . SER B 41 ? 0.8352 0.8330 0.8190 -0.0069 -0.0296 0.0000 40 SER B C 1942 O O . SER B 41 ? 0.7832 0.7870 0.7671 -0.0078 -0.0283 0.0011 40 SER B O 1943 C CB . SER B 41 ? 0.9257 0.9212 0.9113 -0.0090 -0.0358 0.0018 40 SER B CB 1944 O OG . SER B 41 ? 0.9666 0.9645 0.9501 -0.0095 -0.0371 0.0046 40 SER B OG 1945 N N . THR B 42 ? 0.7921 0.7796 0.7717 -0.0036 -0.0298 -0.0002 41 THR B N 1946 C CA . THR B 42 ? 0.7057 0.6871 0.6798 -0.0005 -0.0288 0.0011 41 THR B CA 1947 C C . THR B 42 ? 0.6827 0.6520 0.6506 0.0023 -0.0323 0.0037 41 THR B C 1948 O O . THR B 42 ? 0.7070 0.6712 0.6748 0.0025 -0.0348 0.0034 41 THR B O 1949 C CB . THR B 42 ? 0.7337 0.7137 0.7081 0.0012 -0.0251 -0.0016 41 THR B CB 1950 O OG1 . THR B 42 ? 0.8500 0.8208 0.8227 0.0033 -0.0262 -0.0026 41 THR B OG1 1951 C CG2 . THR B 42 ? 0.7651 0.7566 0.7463 -0.0018 -0.0218 -0.0047 41 THR B CG2 1952 N N . GLN B 43 ? 0.7170 0.6820 0.6798 0.0043 -0.0326 0.0061 42 GLN B N 1953 C CA . GLN B 43 ? 0.6409 0.5942 0.5972 0.0070 -0.0357 0.0087 42 GLN B CA 1954 C C . GLN B 43 ? 0.5570 0.5025 0.5085 0.0105 -0.0338 0.0086 42 GLN B C 1955 O O . GLN B 43 ? 0.5820 0.5320 0.5342 0.0107 -0.0306 0.0080 42 GLN B O 1956 C CB . GLN B 43 ? 0.6272 0.5817 0.5813 0.0062 -0.0381 0.0122 42 GLN B CB 1957 C CG . GLN B 43 ? 0.7840 0.7439 0.7420 0.0032 -0.0407 0.0125 42 GLN B CG 1958 C CD . GLN B 43 ? 0.8386 0.7987 0.7941 0.0026 -0.0433 0.0160 42 GLN B CD 1959 O OE1 . GLN B 43 ? 0.8085 0.7670 0.7603 0.0039 -0.0427 0.0181 42 GLN B OE1 1960 N NE2 . GLN B 43 ? 0.8982 0.8602 0.8558 0.0007 -0.0462 0.0167 42 GLN B NE2 1961 N N . THR B 44 ? 0.6180 0.5519 0.5649 0.0133 -0.0357 0.0092 43 THR B N 1962 C CA . THR B 44 ? 0.4848 0.4103 0.4273 0.0168 -0.0341 0.0089 43 THR B CA 1963 C C . THR B 44 ? 0.4602 0.3854 0.4001 0.0175 -0.0326 0.0108 43 THR B C 1964 O O . THR B 44 ? 0.4792 0.4056 0.4196 0.0162 -0.0333 0.0122 43 THR B O 1965 C CB . THR B 44 ? 0.4819 0.4013 0.4242 0.0176 -0.0343 0.0072 43 THR B CB 1966 O OG1 . THR B 44 ? 0.6707 0.5892 0.6154 0.0173 -0.0359 0.0057 43 THR B OG1 1967 C CG2 . THR B 44 ? 0.4131 0.3301 0.3542 0.0193 -0.0308 0.0056 43 THR B CG2 1968 N N . VAL B 45 ? 0.4244 0.3489 0.3625 0.0192 -0.0297 0.0103 44 VAL B N 1969 C CA . VAL B 45 ? 0.4118 0.3371 0.3491 0.0195 -0.0276 0.0115 44 VAL B CA 1970 C C . VAL B 45 ? 0.4018 0.3231 0.3388 0.0205 -0.0257 0.0097 44 VAL B C 1971 O O . VAL B 45 ? 0.4226 0.3436 0.3600 0.0199 -0.0257 0.0103 44 VAL B O 1972 C CB . VAL B 45 ? 0.4243 0.3527 0.3600 0.0203 -0.0258 0.0126 44 VAL B CB 1973 C CG1 . VAL B 45 ? 0.2625 0.1909 0.1979 0.0208 -0.0233 0.0134 44 VAL B CG1 1974 C CG2 . VAL B 45 ? 0.3788 0.3153 0.3157 0.0179 -0.0274 0.0143 44 VAL B CG2 1975 N N . ALA B 46 ? 0.3533 0.2725 0.2901 0.0219 -0.0240 0.0076 45 ALA B N 1976 C CA . ALA B 46 ? 0.2630 0.1806 0.1998 0.0224 -0.0222 0.0061 45 ALA B CA 1977 C C . ALA B 46 ? 0.3431 0.2596 0.2810 0.0231 -0.0215 0.0039 45 ALA B C 1978 O O . ALA B 46 ? 0.3635 0.2802 0.3019 0.0239 -0.0209 0.0029 45 ALA B O 1979 C CB . ALA B 46 ? 0.3461 0.2644 0.2819 0.0233 -0.0196 0.0065 45 ALA B CB 1980 N N . VAL B 47 ? 0.3794 0.2954 0.3182 0.0228 -0.0213 0.0031 46 VAL B N 1981 C CA . VAL B 47 ? 0.3190 0.2350 0.2598 0.0230 -0.0206 0.0013 46 VAL B CA 1982 C C . VAL B 47 ? 0.3482 0.2649 0.2892 0.0234 -0.0185 0.0010 46 VAL B C 1983 O O . VAL B 47 ? 0.3157 0.2296 0.2524 0.0235 -0.0196 0.0014 46 VAL B O 1984 C CB . VAL B 47 ? 0.3552 0.2704 0.2972 0.0220 -0.0230 0.0011 46 VAL B CB 1985 C CG1 . VAL B 47 ? 0.3857 0.3014 0.3304 0.0221 -0.0225 -0.0006 46 VAL B CG1 1986 C CG2 . VAL B 47 ? 0.3530 0.2676 0.2942 0.0210 -0.0258 0.0024 46 VAL B CG2 1987 N N . HIS B 48 ? 0.3501 0.2680 0.2930 0.0240 -0.0165 -0.0003 47 HIS B N 1988 C CA . HIS B 48 ? 0.3276 0.2427 0.2662 0.0250 -0.0162 -0.0010 47 HIS B CA 1989 C C . HIS B 48 ? 0.3585 0.2737 0.2992 0.0249 -0.0164 -0.0022 47 HIS B C 1990 O O . HIS B 48 ? 0.3875 0.3058 0.3335 0.0245 -0.0150 -0.0031 47 HIS B O 1991 C CB . HIS B 48 ? 0.2816 0.1976 0.2193 0.0260 -0.0138 -0.0012 47 HIS B CB 1992 C CG . HIS B 48 ? 0.3068 0.2198 0.2395 0.0270 -0.0135 -0.0016 47 HIS B CG 1993 N ND1 . HIS B 48 ? 0.3944 0.3077 0.3255 0.0280 -0.0114 -0.0018 47 HIS B ND1 1994 C CD2 . HIS B 48 ? 0.3927 0.3023 0.3216 0.0273 -0.0152 -0.0019 47 HIS B CD2 1995 C CE1 . HIS B 48 ? 0.3623 0.2726 0.2889 0.0288 -0.0117 -0.0020 47 HIS B CE1 1996 N NE2 . HIS B 48 ? 0.3552 0.2631 0.2802 0.0284 -0.0140 -0.0021 47 HIS B NE2 1997 N N . HIS B 49 ? 0.3600 0.2719 0.2969 0.0252 -0.0181 -0.0023 48 HIS B N 1998 C CA . HIS B 49 ? 0.3853 0.2970 0.3237 0.0252 -0.0184 -0.0032 48 HIS B CA 1999 C C . HIS B 49 ? 0.4250 0.3339 0.3587 0.0263 -0.0182 -0.0035 48 HIS B C 2000 O O . HIS B 49 ? 0.4013 0.3069 0.3295 0.0268 -0.0193 -0.0031 48 HIS B O 2001 C CB . HIS B 49 ? 0.3955 0.3061 0.3345 0.0242 -0.0210 -0.0031 48 HIS B CB 2002 C CG . HIS B 49 ? 0.4277 0.3389 0.3695 0.0241 -0.0210 -0.0040 48 HIS B CG 2003 N ND1 . HIS B 49 ? 0.3999 0.3087 0.3388 0.0249 -0.0214 -0.0044 48 HIS B ND1 2004 C CD2 . HIS B 49 ? 0.3515 0.2653 0.2989 0.0232 -0.0206 -0.0046 48 HIS B CD2 2005 C CE1 . HIS B 49 ? 0.3785 0.2885 0.3211 0.0245 -0.0213 -0.0052 48 HIS B CE1 2006 N NE2 . HIS B 49 ? 0.3844 0.2975 0.3322 0.0235 -0.0208 -0.0054 48 HIS B NE2 2007 N N . PRO B 50 ? 0.4583 0.3682 0.3940 0.0268 -0.0167 -0.0043 49 PRO B N 2008 C CA . PRO B 50 ? 0.5300 0.4375 0.4612 0.0280 -0.0162 -0.0044 49 PRO B CA 2009 C C . PRO B 50 ? 0.5408 0.4442 0.4670 0.0282 -0.0186 -0.0043 49 PRO B C 2010 O O . PRO B 50 ? 0.5629 0.4634 0.4838 0.0291 -0.0187 -0.0041 49 PRO B O 2011 C CB . PRO B 50 ? 0.4710 0.3811 0.4067 0.0281 -0.0141 -0.0053 49 PRO B CB 2012 C CG . PRO B 50 ? 0.4582 0.3708 0.3997 0.0270 -0.0145 -0.0059 49 PRO B CG 2013 C CD . PRO B 50 ? 0.4049 0.3185 0.3471 0.0263 -0.0151 -0.0053 49 PRO B CD 2014 N N . GLN B 51 ? 0.4888 0.3918 0.4165 0.0274 -0.0207 -0.0044 50 GLN B N 2015 C CA . GLN B 51 ? 0.5046 0.4036 0.4275 0.0275 -0.0231 -0.0044 50 GLN B CA 2016 C C . GLN B 51 ? 0.5668 0.4639 0.4870 0.0268 -0.0252 -0.0038 50 GLN B C 2017 O O . GLN B 51 ? 0.6325 0.5259 0.5474 0.0272 -0.0267 -0.0038 50 GLN B O 2018 C CB . GLN B 51 ? 0.5229 0.4221 0.4484 0.0271 -0.0243 -0.0048 50 GLN B CB 2019 C CG . GLN B 51 ? 0.5965 0.4976 0.5252 0.0276 -0.0221 -0.0055 50 GLN B CG 2020 C CD . GLN B 51 ? 0.7111 0.6104 0.6356 0.0289 -0.0209 -0.0055 50 GLN B CD 2021 O OE1 . GLN B 51 ? 0.7769 0.6726 0.6957 0.0294 -0.0223 -0.0053 50 GLN B OE1 2022 N NE2 . GLN B 51 ? 0.6124 0.5142 0.5397 0.0293 -0.0183 -0.0058 50 GLN B NE2 2023 N N . TYR B 52 ? 0.5278 0.4273 0.4516 0.0259 -0.0253 -0.0034 51 TYR B N 2024 C CA . TYR B 52 ? 0.4661 0.3642 0.3883 0.0250 -0.0274 -0.0029 51 TYR B CA 2025 C C . TYR B 52 ? 0.4936 0.3917 0.4140 0.0252 -0.0265 -0.0023 51 TYR B C 2026 O O . TYR B 52 ? 0.5465 0.4436 0.4659 0.0245 -0.0279 -0.0017 51 TYR B O 2027 C CB . TYR B 52 ? 0.4698 0.3705 0.3971 0.0238 -0.0283 -0.0026 51 TYR B CB 2028 C CG . TYR B 52 ? 0.4606 0.3616 0.3902 0.0235 -0.0292 -0.0032 51 TYR B CG 2029 C CD1 . TYR B 52 ? 0.5745 0.4722 0.5003 0.0239 -0.0308 -0.0036 51 TYR B CD1 2030 C CD2 . TYR B 52 ? 0.6033 0.5078 0.5389 0.0229 -0.0283 -0.0034 51 TYR B CD2 2031 C CE1 . TYR B 52 ? 0.6716 0.5696 0.5997 0.0236 -0.0316 -0.0040 51 TYR B CE1 2032 C CE2 . TYR B 52 ? 0.5327 0.4375 0.4707 0.0226 -0.0289 -0.0040 51 TYR B CE2 2033 C CZ . TYR B 52 ? 0.5950 0.4966 0.5292 0.0230 -0.0306 -0.0042 51 TYR B CZ 2034 O OH . TYR B 52 ? 0.7266 0.6285 0.6632 0.0227 -0.0313 -0.0047 51 TYR B OH 2035 N N . GLY B 53 ? 0.4463 0.3453 0.3662 0.0261 -0.0241 -0.0023 52 GLY B N 2036 C CA . GLY B 53 ? 0.4384 0.3372 0.3563 0.0264 -0.0232 -0.0017 52 GLY B CA 2037 C C . GLY B 53 ? 0.4082 0.3102 0.3303 0.0255 -0.0227 -0.0009 52 GLY B C 2038 O O . GLY B 53 ? 0.4140 0.3189 0.3410 0.0247 -0.0228 -0.0008 52 GLY B O 2039 N N . PHE B 54 ? 0.3987 0.3002 0.3189 0.0256 -0.0222 -0.0003 53 PHE B N 2040 C CA . PHE B 54 ? 0.3897 0.2943 0.3136 0.0249 -0.0217 0.0008 53 PHE B CA 2041 C C . PHE B 54 ? 0.3852 0.2895 0.3102 0.0236 -0.0241 0.0015 53 PHE B C 2042 O O . PHE B 54 ? 0.4847 0.3857 0.4065 0.0234 -0.0261 0.0012 53 PHE B O 2043 C CB . PHE B 54 ? 0.4725 0.3767 0.3942 0.0254 -0.0204 0.0014 53 PHE B CB 2044 C CG . PHE B 54 ? 0.4596 0.3640 0.3796 0.0267 -0.0180 0.0009 53 PHE B CG 2045 C CD1 . PHE B 54 ? 0.4209 0.3279 0.3440 0.0269 -0.0165 0.0003 53 PHE B CD1 2046 C CD2 . PHE B 54 ? 0.4436 0.3456 0.3591 0.0275 -0.0172 0.0009 53 PHE B CD2 2047 C CE1 . PHE B 54 ? 0.4738 0.3810 0.3954 0.0280 -0.0143 -0.0001 53 PHE B CE1 2048 C CE2 . PHE B 54 ? 0.4659 0.3681 0.3797 0.0286 -0.0150 0.0005 53 PHE B CE2 2049 C CZ . PHE B 54 ? 0.4950 0.3998 0.4118 0.0288 -0.0136 0.0001 53 PHE B CZ 2050 N N . SER B 55 ? 0.3929 0.3007 0.3223 0.0227 -0.0239 0.0026 54 SER B N 2051 C CA . SER B 55 ? 0.3570 0.2651 0.2875 0.0215 -0.0259 0.0037 54 SER B CA 2052 C C . SER B 55 ? 0.3506 0.2628 0.2846 0.0209 -0.0248 0.0055 54 SER B C 2053 O O . SER B 55 ? 0.3766 0.2922 0.3141 0.0211 -0.0231 0.0056 54 SER B O 2054 C CB . SER B 55 ? 0.4167 0.3253 0.3497 0.0205 -0.0276 0.0033 54 SER B CB 2055 O OG . SER B 55 ? 0.3677 0.2779 0.3029 0.0192 -0.0293 0.0046 54 SER B OG 2056 N N . VAL B 56 ? 0.3516 0.2636 0.2846 0.0203 -0.0258 0.0068 55 VAL B N 2057 C CA . VAL B 56 ? 0.2963 0.2128 0.2326 0.0197 -0.0251 0.0090 55 VAL B CA 2058 C C . VAL B 56 ? 0.3631 0.2811 0.3011 0.0182 -0.0273 0.0103 55 VAL B C 2059 O O . VAL B 56 ? 0.4871 0.4015 0.4225 0.0179 -0.0291 0.0097 55 VAL B O 2060 C CB . VAL B 56 ? 0.3398 0.2557 0.2738 0.0203 -0.0240 0.0098 55 VAL B CB 2061 C CG1 . VAL B 56 ? 0.3744 0.2957 0.3117 0.0195 -0.0234 0.0124 55 VAL B CG1 2062 C CG2 . VAL B 56 ? 0.2878 0.2020 0.2196 0.0217 -0.0219 0.0084 55 VAL B CG2 2063 N N . GLN B 57 ? 0.3801 0.3000 0.3188 0.0176 -0.0285 0.0113 56 GLN B N 2064 C CA . GLN B 57 ? 0.4091 0.3302 0.3490 0.0161 -0.0311 0.0122 56 GLN B CA 2065 C C . GLN B 57 ? 0.3447 0.2698 0.2854 0.0152 -0.0314 0.0147 56 GLN B C 2066 O O . GLN B 57 ? 0.4006 0.3281 0.3410 0.0156 -0.0299 0.0158 56 GLN B O 2067 C CB . GLN B 57 ? 0.3592 0.2800 0.2998 0.0157 -0.0331 0.0113 56 GLN B CB 2068 C CG . GLN B 57 ? 0.3968 0.3151 0.3379 0.0152 -0.0346 0.0099 56 GLN B CG 2069 C CD . GLN B 57 ? 0.4451 0.3608 0.3852 0.0164 -0.0328 0.0081 56 GLN B CD 2070 O OE1 . GLN B 57 ? 0.5505 0.4660 0.4902 0.0176 -0.0310 0.0072 56 GLN B OE1 2071 N NE2 . GLN B 57 ? 0.4759 0.3903 0.4158 0.0160 -0.0333 0.0077 56 GLN B NE2 2072 N N . GLY B 58 ? 0.3588 0.2852 0.3005 0.0138 -0.0334 0.0156 57 GLY B N 2073 C CA . GLY B 58 ? 0.3568 0.2882 0.2998 0.0125 -0.0341 0.0179 57 GLY B CA 2074 C C . GLY B 58 ? 0.4591 0.3924 0.4021 0.0130 -0.0320 0.0195 57 GLY B C 2075 O O . GLY B 58 ? 0.4884 0.4191 0.4308 0.0139 -0.0306 0.0191 57 GLY B O 2076 N N . ASP B 59 ? 0.4738 0.4125 0.4176 0.0124 -0.0318 0.0215 58 ASP B N 2077 C CA . ASP B 59 ? 0.4625 0.4036 0.4066 0.0128 -0.0298 0.0232 58 ASP B CA 2078 C C . ASP B 59 ? 0.3878 0.3274 0.3309 0.0142 -0.0275 0.0227 58 ASP B C 2079 O O . ASP B 59 ? 0.4208 0.3630 0.3645 0.0145 -0.0258 0.0242 58 ASP B O 2080 C CB . ASP B 59 ? 0.5006 0.4487 0.4461 0.0116 -0.0302 0.0255 58 ASP B CB 2081 C CG . ASP B 59 ? 0.6063 0.5587 0.5515 0.0112 -0.0302 0.0259 58 ASP B CG 2082 O OD1 . ASP B 59 ? 0.6138 0.5652 0.5579 0.0123 -0.0284 0.0256 58 ASP B OD1 2083 O OD2 . ASP B 59 ? 0.5748 0.5322 0.5210 0.0095 -0.0319 0.0264 58 ASP B OD2 2084 N N . TYR B 60 ? 0.3460 0.2819 0.2877 0.0151 -0.0273 0.0206 59 TYR B N 2085 C CA . TYR B 60 ? 0.3527 0.2868 0.2934 0.0165 -0.0251 0.0198 59 TYR B CA 2086 C C . TYR B 60 ? 0.3603 0.2899 0.3000 0.0174 -0.0242 0.0184 59 TYR B C 2087 O O . TYR B 60 ? 0.3888 0.3163 0.3266 0.0185 -0.0226 0.0178 59 TYR B O 2088 C CB . TYR B 60 ? 0.3494 0.2815 0.2888 0.0173 -0.0251 0.0180 59 TYR B CB 2089 C CG . TYR B 60 ? 0.3553 0.2919 0.2946 0.0166 -0.0259 0.0191 59 TYR B CG 2090 C CD1 . TYR B 60 ? 0.3629 0.3030 0.3016 0.0169 -0.0243 0.0203 59 TYR B CD1 2091 C CD2 . TYR B 60 ? 0.3774 0.3157 0.3173 0.0153 -0.0285 0.0191 59 TYR B CD2 2092 C CE1 . TYR B 60 ? 0.3884 0.3340 0.3267 0.0159 -0.0250 0.0213 59 TYR B CE1 2093 C CE2 . TYR B 60 ? 0.3740 0.3182 0.3140 0.0141 -0.0295 0.0201 59 TYR B CE2 2094 C CZ . TYR B 60 ? 0.3812 0.3292 0.3201 0.0144 -0.0277 0.0211 59 TYR B CZ 2095 O OH . TYR B 60 ? 0.4446 0.3999 0.3832 0.0128 -0.0284 0.0218 59 TYR B OH 2096 N N . GLN B 61 ? 0.3310 0.2566 0.2690 0.0170 -0.0261 0.0175 60 GLN B N 2097 C CA . GLN B 61 ? 0.4104 0.3291 0.3439 0.0179 -0.0265 0.0155 60 GLN B CA 2098 C C . GLN B 61 ? 0.4689 0.3867 0.4003 0.0184 -0.0256 0.0165 60 GLN B C 2099 O O . GLN B 61 ? 0.4606 0.3818 0.3937 0.0176 -0.0258 0.0187 60 GLN B O 2100 C CB . GLN B 61 ? 0.3672 0.2827 0.2993 0.0172 -0.0289 0.0147 60 GLN B CB 2101 C CG . GLN B 61 ? 0.3776 0.2944 0.3121 0.0166 -0.0299 0.0140 60 GLN B CG 2102 C CD . GLN B 61 ? 0.4166 0.3294 0.3492 0.0160 -0.0323 0.0129 60 GLN B CD 2103 O OE1 . GLN B 61 ? 0.4231 0.3308 0.3517 0.0167 -0.0328 0.0112 60 GLN B OE1 2104 N NE2 . GLN B 61 ? 0.4253 0.3406 0.3604 0.0146 -0.0339 0.0138 60 GLN B NE2 2105 N N . GLY B 62 ? 0.4109 0.3243 0.3387 0.0197 -0.0246 0.0149 61 GLY B N 2106 C CA . GLY B 62 ? 0.3086 0.2209 0.2344 0.0203 -0.0235 0.0156 61 GLY B CA 2107 C C . GLY B 62 ? 0.3525 0.2691 0.2805 0.0207 -0.0214 0.0170 61 GLY B C 2108 O O . GLY B 62 ? 0.4381 0.3536 0.3644 0.0214 -0.0202 0.0173 61 GLY B O 2109 N N . ARG B 63 ? 0.4146 0.3362 0.3464 0.0202 -0.0208 0.0177 62 ARG B N 2110 C CA . ARG B 63 ? 0.4405 0.3667 0.3745 0.0203 -0.0189 0.0190 62 ARG B CA 2111 C C . ARG B 63 ? 0.4055 0.3321 0.3402 0.0211 -0.0174 0.0175 62 ARG B C 2112 O O . ARG B 63 ? 0.3901 0.3210 0.3268 0.0211 -0.0159 0.0186 62 ARG B O 2113 C CB . ARG B 63 ? 0.3626 0.2963 0.3008 0.0187 -0.0193 0.0219 62 ARG B CB 2114 C CG . ARG B 63 ? 0.3504 0.2847 0.2886 0.0178 -0.0208 0.0235 62 ARG B CG 2115 C CD . ARG B 63 ? 0.4489 0.3915 0.3907 0.0164 -0.0209 0.0264 62 ARG B CD 2116 N NE . ARG B 63 ? 0.4570 0.4043 0.4014 0.0155 -0.0216 0.0266 62 ARG B NE 2117 C CZ . ARG B 63 ? 0.4277 0.3785 0.3715 0.0152 -0.0215 0.0272 62 ARG B CZ 2118 N NH1 . ARG B 63 ? 0.3905 0.3439 0.3344 0.0154 -0.0198 0.0281 62 ARG B NH1 2119 N NH2 . ARG B 63 ? 0.3147 0.2667 0.2577 0.0145 -0.0233 0.0266 62 ARG B NH2 2120 N N . VAL B 64 ? 0.3599 0.2827 0.2930 0.0217 -0.0178 0.0151 63 VAL B N 2121 C CA . VAL B 64 ? 0.3682 0.2914 0.3021 0.0224 -0.0165 0.0136 63 VAL B CA 2122 C C . VAL B 64 ? 0.3456 0.2632 0.2750 0.0239 -0.0157 0.0111 63 VAL B C 2123 O O . VAL B 64 ? 0.3768 0.2903 0.3032 0.0240 -0.0171 0.0099 63 VAL B O 2124 C CB . VAL B 64 ? 0.3962 0.3211 0.3328 0.0217 -0.0176 0.0133 63 VAL B CB 2125 C CG1 . VAL B 64 ? 0.3390 0.2621 0.2742 0.0230 -0.0164 0.0112 63 VAL B CG1 2126 C CG2 . VAL B 64 ? 0.3581 0.2863 0.2951 0.0209 -0.0190 0.0154 63 VAL B CG2 2127 N N . LEU B 65 ? 0.3599 0.2778 0.2886 0.0250 -0.0135 0.0103 64 LEU B N 2128 C CA . LEU B 65 ? 0.3827 0.2965 0.3072 0.0263 -0.0126 0.0081 64 LEU B CA 2129 C C . LEU B 65 ? 0.4108 0.3264 0.3372 0.0267 -0.0113 0.0069 64 LEU B C 2130 O O . LEU B 65 ? 0.4792 0.3988 0.4090 0.0266 -0.0100 0.0076 64 LEU B O 2131 C CB . LEU B 65 ? 0.3989 0.3112 0.3203 0.0273 -0.0109 0.0080 64 LEU B CB 2132 C CG . LEU B 65 ? 0.4469 0.3569 0.3660 0.0272 -0.0118 0.0089 64 LEU B CG 2133 C CD1 . LEU B 65 ? 0.2765 0.1851 0.1926 0.0284 -0.0098 0.0087 64 LEU B CD1 2134 C CD2 . LEU B 65 ? 0.4925 0.3980 0.4081 0.0271 -0.0138 0.0078 64 LEU B CD2 2135 N N . PHE B 66 ? 0.4254 0.3383 0.3496 0.0272 -0.0118 0.0052 65 PHE B N 2136 C CA . PHE B 66 ? 0.3986 0.3127 0.3237 0.0278 -0.0102 0.0040 65 PHE B CA 2137 C C . PHE B 66 ? 0.4439 0.3567 0.3653 0.0290 -0.0081 0.0035 65 PHE B C 2138 O O . PHE B 66 ? 0.4841 0.3933 0.4008 0.0296 -0.0085 0.0031 65 PHE B O 2139 C CB . PHE B 66 ? 0.3920 0.3041 0.3163 0.0277 -0.0115 0.0027 65 PHE B CB 2140 C CG . PHE B 66 ? 0.4786 0.3934 0.4079 0.0268 -0.0123 0.0027 65 PHE B CG 2141 C CD1 . PHE B 66 ? 0.3745 0.2929 0.3081 0.0268 -0.0105 0.0023 65 PHE B CD1 2142 C CD2 . PHE B 66 ? 0.4751 0.3890 0.4051 0.0258 -0.0147 0.0030 65 PHE B CD2 2143 C CE1 . PHE B 66 ? 0.3136 0.2334 0.2507 0.0263 -0.0112 0.0019 65 PHE B CE1 2144 C CE2 . PHE B 66 ? 0.4184 0.3349 0.3532 0.0249 -0.0153 0.0031 65 PHE B CE2 2145 C CZ . PHE B 66 ? 0.3955 0.3140 0.3328 0.0254 -0.0138 0.0023 65 PHE B CZ 2146 N N . LYS B 67 ? 0.4150 0.3309 0.3386 0.0294 -0.0060 0.0034 66 LYS B N 2147 C CA . LYS B 67 ? 0.4200 0.3353 0.3405 0.0305 -0.0038 0.0031 66 LYS B CA 2148 C C . LYS B 67 ? 0.5519 0.4637 0.4677 0.0313 -0.0039 0.0021 66 LYS B C 2149 O O . LYS B 67 ? 0.4984 0.4073 0.4095 0.0321 -0.0034 0.0020 66 LYS B O 2150 C CB . LYS B 67 ? 0.4540 0.3733 0.3780 0.0306 -0.0017 0.0032 66 LYS B CB 2151 C CG . LYS B 67 ? 0.4403 0.3596 0.3615 0.0316 0.0007 0.0031 66 LYS B CG 2152 C CD . LYS B 67 ? 0.4631 0.3862 0.3880 0.0316 0.0026 0.0029 66 LYS B CD 2153 C CE . LYS B 67 ? 0.4849 0.4085 0.4075 0.0324 0.0050 0.0033 66 LYS B CE 2154 N NZ . LYS B 67 ? 0.4907 0.4152 0.4133 0.0325 0.0054 0.0042 66 LYS B NZ 2155 N N . ASN B 68 ? 0.4696 0.3817 0.3869 0.0311 -0.0044 0.0014 67 ASN B N 2156 C CA . ASN B 68 ? 0.5168 0.4261 0.4303 0.0318 -0.0045 0.0007 67 ASN B CA 2157 C C . ASN B 68 ? 0.5027 0.4122 0.4187 0.0313 -0.0059 0.0001 67 ASN B C 2158 O O . ASN B 68 ? 0.5348 0.4468 0.4556 0.0304 -0.0065 0.0001 67 ASN B O 2159 C CB . ASN B 68 ? 0.5321 0.4426 0.4448 0.0326 -0.0020 0.0007 67 ASN B CB 2160 C CG . ASN B 68 ? 0.5722 0.4872 0.4905 0.0322 -0.0005 0.0008 67 ASN B CG 2161 O OD1 . ASN B 68 ? 0.5863 0.5030 0.5089 0.0315 -0.0011 0.0002 67 ASN B OD1 2162 N ND2 . ASN B 68 ? 0.5122 0.4292 0.4310 0.0325 0.0015 0.0013 67 ASN B ND2 2163 N N . TYR B 69 ? 0.4592 0.3661 0.3721 0.0318 -0.0063 -0.0004 68 TYR B N 2164 C CA . TYR B 69 ? 0.4734 0.3797 0.3876 0.0315 -0.0079 -0.0010 68 TYR B CA 2165 C C . TYR B 69 ? 0.5708 0.4802 0.4899 0.0313 -0.0067 -0.0015 68 TYR B C 2166 O O . TYR B 69 ? 0.5923 0.5015 0.5133 0.0309 -0.0079 -0.0020 68 TYR B O 2167 C CB . TYR B 69 ? 0.4604 0.3624 0.3689 0.0322 -0.0088 -0.0013 68 TYR B CB 2168 C CG . TYR B 69 ? 0.4736 0.3722 0.3782 0.0321 -0.0108 -0.0012 68 TYR B CG 2169 C CD1 . TYR B 69 ? 0.5483 0.4460 0.4541 0.0313 -0.0131 -0.0014 68 TYR B CD1 2170 C CD2 . TYR B 69 ? 0.4841 0.3802 0.3840 0.0328 -0.0103 -0.0010 68 TYR B CD2 2171 C CE1 . TYR B 69 ? 0.6674 0.5619 0.5697 0.0311 -0.0150 -0.0014 68 TYR B CE1 2172 C CE2 . TYR B 69 ? 0.5255 0.4183 0.4220 0.0326 -0.0120 -0.0011 68 TYR B CE2 2173 C CZ . TYR B 69 ? 0.5059 0.3978 0.4036 0.0317 -0.0144 -0.0013 68 TYR B CZ 2174 O OH . TYR B 69 ? 0.5812 0.4698 0.4758 0.0315 -0.0162 -0.0013 68 TYR B OH 2175 N N . SER B 70 ? 0.5395 0.4516 0.4606 0.0315 -0.0044 -0.0014 69 SER B N 2176 C CA . SER B 70 ? 0.3637 0.2788 0.2900 0.0313 -0.0031 -0.0021 69 SER B CA 2177 C C . SER B 70 ? 0.4983 0.4163 0.4306 0.0302 -0.0037 -0.0027 69 SER B C 2178 O O . SER B 70 ? 0.5587 0.4784 0.4930 0.0296 -0.0037 -0.0024 69 SER B O 2179 C CB . SER B 70 ? 0.4730 0.3906 0.4006 0.0316 -0.0005 -0.0019 69 SER B CB 2180 O OG . SER B 70 ? 0.5694 0.4902 0.5025 0.0312 0.0008 -0.0029 69 SER B OG 2181 N N . LEU B 71 ? 0.5208 0.4394 0.4563 0.0298 -0.0040 -0.0037 70 LEU B N 2182 C CA . LEU B 71 ? 0.4607 0.3823 0.4024 0.0287 -0.0041 -0.0047 70 LEU B CA 2183 C C . LEU B 71 ? 0.4385 0.3647 0.3856 0.0282 -0.0017 -0.0056 70 LEU B C 2184 O O . LEU B 71 ? 0.4417 0.3706 0.3937 0.0273 -0.0017 -0.0066 70 LEU B O 2185 C CB . LEU B 71 ? 0.4740 0.3955 0.4181 0.0284 -0.0046 -0.0057 70 LEU B CB 2186 C CG . LEU B 71 ? 0.4814 0.4003 0.4240 0.0281 -0.0073 -0.0054 70 LEU B CG 2187 C CD1 . LEU B 71 ? 0.4911 0.4057 0.4265 0.0288 -0.0091 -0.0043 70 LEU B CD1 2188 C CD2 . LEU B 71 ? 0.4847 0.4040 0.4301 0.0279 -0.0072 -0.0065 70 LEU B CD2 2189 N N . ASN B 72 ? 0.4751 0.4023 0.4216 0.0288 0.0003 -0.0056 71 ASN B N 2190 C CA . ASN B 72 ? 0.5113 0.4432 0.4629 0.0282 0.0026 -0.0068 71 ASN B CA 2191 C C . ASN B 72 ? 0.5728 0.5054 0.5232 0.0284 0.0030 -0.0059 71 ASN B C 2192 O O . ASN B 72 ? 0.5181 0.4549 0.4724 0.0279 0.0049 -0.0070 71 ASN B O 2193 C CB . ASN B 72 ? 0.4730 0.4060 0.4253 0.0286 0.0046 -0.0074 71 ASN B CB 2194 C CG . ASN B 72 ? 0.6223 0.5568 0.5789 0.0280 0.0050 -0.0092 71 ASN B CG 2195 O OD1 . ASN B 72 ? 0.6382 0.5698 0.5927 0.0283 0.0035 -0.0088 71 ASN B OD1 2196 N ND2 . ASN B 72 ? 0.6579 0.5973 0.6206 0.0271 0.0070 -0.0114 71 ASN B ND2 2197 N N . ASP B 73 ? 0.5577 0.4869 0.5030 0.0289 0.0012 -0.0041 72 ASP B N 2198 C CA . ASP B 73 ? 0.4966 0.4261 0.4401 0.0291 0.0014 -0.0029 72 ASP B CA 2199 C C . ASP B 73 ? 0.4788 0.4070 0.4220 0.0285 -0.0009 -0.0021 72 ASP B C 2200 O O . ASP B 73 ? 0.4966 0.4210 0.4351 0.0288 -0.0028 -0.0012 72 ASP B O 2201 C CB . ASP B 73 ? 0.4436 0.3702 0.3808 0.0301 0.0018 -0.0015 72 ASP B CB 2202 C CG . ASP B 73 ? 0.3852 0.3128 0.3213 0.0303 0.0027 -0.0005 72 ASP B CG 2203 O OD1 . ASP B 73 ? 0.4014 0.3307 0.3401 0.0298 0.0021 -0.0002 72 ASP B OD1 2204 O OD2 . ASP B 73 ? 0.5394 0.4663 0.4723 0.0311 0.0041 0.0002 72 ASP B OD2 2205 N N . ALA B 74 ? 0.4237 0.3518 0.3670 0.0290 -0.0010 -0.0027 73 ALA B N 2206 C CA . ALA B 74 ? 0.3752 0.3005 0.3159 0.0291 -0.0035 -0.0018 73 ALA B CA 2207 C C . ALA B 74 ? 0.3667 0.2905 0.3032 0.0298 -0.0038 0.0000 73 ALA B C 2208 O O . ALA B 74 ? 0.3998 0.3221 0.3348 0.0298 -0.0059 0.0010 73 ALA B O 2209 C CB . ALA B 74 ? 0.2937 0.2194 0.2364 0.0292 -0.0036 -0.0036 73 ALA B CB 2210 N N . THR B 75 ? 0.3282 0.2530 0.2634 0.0303 -0.0020 0.0007 74 THR B N 2211 C CA . THR B 75 ? 0.3343 0.2585 0.2664 0.0310 -0.0019 0.0024 74 THR B CA 2212 C C . THR B 75 ? 0.3367 0.2597 0.2682 0.0297 -0.0044 0.0038 74 THR B C 2213 O O . THR B 75 ? 0.3222 0.2448 0.2546 0.0288 -0.0051 0.0036 74 THR B O 2214 C CB . THR B 75 ? 0.4270 0.3527 0.3583 0.0315 0.0006 0.0026 74 THR B CB 2215 O OG1 . THR B 75 ? 0.4211 0.3490 0.3540 0.0323 0.0032 0.0014 74 THR B OG1 2216 C CG2 . THR B 75 ? 0.3016 0.2273 0.2305 0.0320 0.0009 0.0045 74 THR B CG2 2217 N N . ILE B 76 ? 0.3176 0.2407 0.2482 0.0296 -0.0058 0.0056 75 ILE B N 2218 C CA . ILE B 76 ? 0.3522 0.2754 0.2834 0.0282 -0.0077 0.0072 75 ILE B CA 2219 C C . ILE B 76 ? 0.3732 0.2986 0.3038 0.0282 -0.0070 0.0093 75 ILE B C 2220 O O . ILE B 76 ? 0.3612 0.2883 0.2907 0.0292 -0.0055 0.0099 75 ILE B O 2221 C CB . ILE B 76 ? 0.3506 0.2733 0.2826 0.0270 -0.0106 0.0079 75 ILE B CB 2222 C CG1 . ILE B 76 ? 0.4131 0.3376 0.3443 0.0273 -0.0113 0.0093 75 ILE B CG1 2223 C CG2 . ILE B 76 ? 0.3272 0.2480 0.2601 0.0269 -0.0114 0.0059 75 ILE B CG2 2224 C CD1 . ILE B 76 ? 0.2630 0.1882 0.1950 0.0257 -0.0145 0.0105 75 ILE B CD1 2225 N N . THR B 77 ? 0.4148 0.3408 0.3466 0.0270 -0.0079 0.0106 76 THR B N 2226 C CA . THR B 77 ? 0.3560 0.2851 0.2886 0.0263 -0.0077 0.0130 76 THR B CA 2227 C C . THR B 77 ? 0.4005 0.3311 0.3348 0.0246 -0.0102 0.0149 76 THR B C 2228 O O . THR B 77 ? 0.3375 0.2662 0.2726 0.0240 -0.0115 0.0143 76 THR B O 2229 C CB . THR B 77 ? 0.4005 0.3297 0.3336 0.0265 -0.0062 0.0129 76 THR B CB 2230 O OG1 . THR B 77 ? 0.4781 0.4021 0.4078 0.0269 -0.0070 0.0116 76 THR B OG1 2231 C CG2 . THR B 77 ? 0.3173 0.2457 0.2487 0.0280 -0.0036 0.0112 76 THR B CG2 2232 N N . LEU B 78 ? 0.4044 0.3393 0.3392 0.0238 -0.0107 0.0173 77 LEU B N 2233 C CA . LEU B 78 ? 0.4421 0.3800 0.3786 0.0220 -0.0129 0.0195 77 LEU B CA 2234 C C . LEU B 78 ? 0.4214 0.3627 0.3598 0.0210 -0.0124 0.0217 77 LEU B C 2235 O O . LEU B 78 ? 0.4354 0.3788 0.3736 0.0214 -0.0107 0.0223 77 LEU B O 2236 C CB . LEU B 78 ? 0.3702 0.3120 0.3059 0.0213 -0.0140 0.0206 77 LEU B CB 2237 C CG . LEU B 78 ? 0.4344 0.3801 0.3717 0.0193 -0.0165 0.0226 77 LEU B CG 2238 C CD1 . LEU B 78 ? 0.3912 0.3326 0.3293 0.0191 -0.0181 0.0215 77 LEU B CD1 2239 C CD2 . LEU B 78 ? 0.4115 0.3613 0.3474 0.0185 -0.0175 0.0228 77 LEU B CD2 2240 N N . HIS B 79 ? 0.3766 0.3185 0.3170 0.0199 -0.0137 0.0229 78 HIS B N 2241 C CA . HIS B 79 ? 0.4086 0.3502 0.3482 0.0199 -0.0134 0.0243 78 HIS B CA 2242 C C . HIS B 79 ? 0.3865 0.3325 0.3281 0.0182 -0.0151 0.0268 78 HIS B C 2243 O O . HIS B 79 ? 0.3508 0.2985 0.2937 0.0174 -0.0165 0.0270 78 HIS B O 2244 C CB . HIS B 79 ? 0.3496 0.2832 0.2850 0.0215 -0.0133 0.0221 78 HIS B CB 2245 C CG . HIS B 79 ? 0.3925 0.3221 0.3254 0.0231 -0.0116 0.0194 78 HIS B CG 2246 N ND1 . HIS B 79 ? 0.4042 0.3317 0.3348 0.0244 -0.0098 0.0188 78 HIS B ND1 2247 C CD2 . HIS B 79 ? 0.3760 0.3037 0.3085 0.0237 -0.0115 0.0173 78 HIS B CD2 2248 C CE1 . HIS B 79 ? 0.3549 0.2796 0.2836 0.0257 -0.0085 0.0163 78 HIS B CE1 2249 N NE2 . HIS B 79 ? 0.3959 0.3207 0.3257 0.0253 -0.0095 0.0154 78 HIS B NE2 2250 N N . ASN B 80 ? 0.4255 0.3733 0.3671 0.0178 -0.0147 0.0287 79 ASN B N 2251 C CA . ASN B 80 ? 0.3517 0.3044 0.2953 0.0164 -0.0159 0.0313 79 ASN B CA 2252 C C . ASN B 80 ? 0.3736 0.3347 0.3204 0.0147 -0.0165 0.0329 79 ASN B C 2253 O O . ASN B 80 ? 0.4485 0.4115 0.3962 0.0141 -0.0177 0.0334 79 ASN B O 2254 C CB . ASN B 80 ? 0.5728 0.5201 0.5144 0.0168 -0.0174 0.0305 79 ASN B CB 2255 C CG . ASN B 80 ? 0.6415 0.5820 0.5796 0.0181 -0.0170 0.0294 79 ASN B CG 2256 O OD1 . ASN B 80 ? 0.6928 0.6320 0.6297 0.0190 -0.0154 0.0290 79 ASN B OD1 2257 N ND2 . ASN B 80 ? 0.6354 0.5717 0.5715 0.0182 -0.0183 0.0289 79 ASN B ND2 2258 N N . ILE B 81 ? 0.3756 0.3402 0.3224 0.0142 -0.0156 0.0330 80 ILE B N 2259 C CA . ILE B 81 ? 0.2867 0.2560 0.2324 0.0133 -0.0164 0.0334 80 ILE B CA 2260 C C . ILE B 81 ? 0.3196 0.2966 0.2674 0.0118 -0.0172 0.0359 80 ILE B C 2261 O O . ILE B 81 ? 0.3590 0.3399 0.3090 0.0109 -0.0165 0.0378 80 ILE B O 2262 C CB . ILE B 81 ? 0.3226 0.2939 0.2664 0.0132 -0.0149 0.0330 80 ILE B CB 2263 C CG1 . ILE B 81 ? 0.4401 0.4047 0.3813 0.0155 -0.0138 0.0300 80 ILE B CG1 2264 C CG2 . ILE B 81 ? 0.2710 0.2502 0.2143 0.0111 -0.0156 0.0340 80 ILE B CG2 2265 C CD1 . ILE B 81 ? 0.5164 0.4816 0.4560 0.0163 -0.0114 0.0293 80 ILE B CD1 2266 N N . GLY B 82 ? 0.3142 0.2932 0.2612 0.0116 -0.0185 0.0354 81 GLY B N 2267 C CA . GLY B 82 ? 0.2421 0.2274 0.1895 0.0117 -0.0186 0.0362 81 GLY B CA 2268 C C . GLY B 82 ? 0.2765 0.2643 0.2206 0.0112 -0.0197 0.0343 81 GLY B C 2269 O O . GLY B 82 ? 0.2344 0.2224 0.1777 0.0104 -0.0199 0.0335 81 GLY B O 2270 N N . PHE B 83 ? 0.3098 0.2996 0.2534 0.0093 -0.0214 0.0337 82 PHE B N 2271 C CA . PHE B 83 ? 0.3525 0.3511 0.2994 0.0048 -0.0226 0.0332 82 PHE B CA 2272 C C . PHE B 83 ? 0.3260 0.3252 0.2739 0.0036 -0.0245 0.0321 82 PHE B C 2273 O O . PHE B 83 ? 0.4491 0.4555 0.3991 0.0012 -0.0240 0.0315 82 PHE B O 2274 C CB . PHE B 83 ? 0.3008 0.3063 0.2515 0.0020 -0.0235 0.0339 82 PHE B CB 2275 C CG . PHE B 83 ? 0.2899 0.2974 0.2408 0.0020 -0.0217 0.0349 82 PHE B CG 2276 C CD1 . PHE B 83 ? 0.2707 0.2848 0.2233 0.0006 -0.0193 0.0351 82 PHE B CD1 2277 C CD2 . PHE B 83 ? 0.2931 0.2966 0.2428 0.0032 -0.0221 0.0355 82 PHE B CD2 2278 C CE1 . PHE B 83 ? 0.2783 0.2944 0.2316 0.0004 -0.0177 0.0361 82 PHE B CE1 2279 C CE2 . PHE B 83 ? 0.2941 0.2992 0.2440 0.0030 -0.0205 0.0364 82 PHE B CE2 2280 C CZ . PHE B 83 ? 0.3329 0.3443 0.2849 0.0015 -0.0185 0.0368 82 PHE B CZ 2281 N N . SER B 84 ? 0.3427 0.3356 0.2899 0.0052 -0.0261 0.0318 83 SER B N 2282 C CA . SER B 84 ? 0.3148 0.3068 0.2629 0.0038 -0.0284 0.0305 83 SER B CA 2283 C C . SER B 84 ? 0.3218 0.3090 0.2673 0.0050 -0.0277 0.0293 83 SER B C 2284 O O . SER B 84 ? 0.4229 0.4108 0.3701 0.0038 -0.0285 0.0271 83 SER B O 2285 C CB . SER B 84 ? 0.2941 0.2798 0.2424 0.0050 -0.0299 0.0302 83 SER B CB 2286 O OG . SER B 84 ? 0.3458 0.3234 0.2924 0.0078 -0.0284 0.0303 83 SER B OG 2287 N N . ASP B 85 ? 0.2891 0.2724 0.2323 0.0076 -0.0251 0.0299 84 ASP B N 2288 C CA . ASP B 85 ? 0.3146 0.2926 0.2548 0.0092 -0.0241 0.0282 84 ASP B CA 2289 C C . ASP B 85 ? 0.3302 0.3188 0.2753 0.0070 -0.0210 0.0256 84 ASP B C 2290 O O . ASP B 85 ? 0.3525 0.3394 0.2982 0.0082 -0.0187 0.0229 84 ASP B O 2291 C CB . ASP B 85 ? 0.2592 0.2321 0.1990 0.0117 -0.0213 0.0287 84 ASP B CB 2292 C CG . ASP B 85 ? 0.3671 0.3332 0.3083 0.0129 -0.0218 0.0286 84 ASP B CG 2293 O OD1 . ASP B 85 ? 0.4770 0.4394 0.4183 0.0129 -0.0236 0.0273 84 ASP B OD1 2294 O OD2 . ASP B 85 ? 0.4230 0.3880 0.3654 0.0135 -0.0203 0.0297 84 ASP B OD2 2295 N N . SER B 86 ? 0.3313 0.3314 0.2806 0.0038 -0.0205 0.0261 85 SER B N 2296 C CA . SER B 86 ? 0.3751 0.3860 0.3300 0.0015 -0.0173 0.0232 85 SER B CA 2297 C C . SER B 86 ? 0.3591 0.3727 0.3185 -0.0003 -0.0177 0.0198 85 SER B C 2298 O O . SER B 86 ? 0.4315 0.4425 0.3911 -0.0009 -0.0207 0.0201 85 SER B O 2299 C CB . SER B 86 ? 0.2818 0.3042 0.2398 -0.0015 -0.0165 0.0248 85 SER B CB 2300 O OG . SER B 86 ? 0.4026 0.4298 0.3634 -0.0041 -0.0191 0.0254 85 SER B OG 2301 N N . GLY B 87 ? 0.2844 0.3032 0.2474 -0.0012 -0.0146 0.0166 86 GLY B N 2302 C CA . GLY B 87 ? 0.2981 0.3210 0.2660 -0.0032 -0.0145 0.0133 86 GLY B CA 2303 C C . GLY B 87 ? 0.3326 0.3522 0.3009 -0.0016 -0.0119 0.0101 86 GLY B C 2304 O O . GLY B 87 ? 0.3213 0.3376 0.2869 0.0006 -0.0097 0.0102 86 GLY B O 2305 N N . LYS B 88 ? 0.3895 0.4100 0.3613 -0.0027 -0.0121 0.0072 87 LYS B N 2306 C CA . LYS B 88 ? 0.3786 0.3972 0.3518 -0.0016 -0.0095 0.0038 87 LYS B CA 2307 C C . LYS B 88 ? 0.4026 0.4086 0.3719 0.0015 -0.0114 0.0037 87 LYS B C 2308 O O . LYS B 88 ? 0.4741 0.4769 0.4433 0.0011 -0.0145 0.0042 87 LYS B O 2309 C CB . LYS B 88 ? 0.4011 0.4295 0.3810 -0.0050 -0.0079 0.0006 87 LYS B CB 2310 C CG . LYS B 88 ? 0.4765 0.5042 0.4584 -0.0042 -0.0048 -0.0031 87 LYS B CG 2311 C CD . LYS B 88 ? 0.5672 0.6056 0.5559 -0.0078 -0.0028 -0.0062 87 LYS B CD 2312 C CE . LYS B 88 ? 0.7260 0.7753 0.7175 -0.0101 0.0001 -0.0064 87 LYS B CE 2313 N NZ . LYS B 88 ? 0.7848 0.8439 0.7827 -0.0133 0.0026 -0.0098 87 LYS B NZ 2314 N N . TYR B 89 ? 0.3653 0.3644 0.3313 0.0046 -0.0096 0.0030 88 TYR B N 2315 C CA . TYR B 89 ? 0.3583 0.3453 0.3203 0.0079 -0.0110 0.0026 88 TYR B CA 2316 C C . TYR B 89 ? 0.4395 0.4273 0.4048 0.0080 -0.0083 -0.0014 88 TYR B C 2317 O O . TYR B 89 ? 0.4406 0.4364 0.4096 0.0067 -0.0049 -0.0035 88 TYR B O 2318 C CB . TYR B 89 ? 0.2717 0.2493 0.2272 0.0115 -0.0109 0.0049 88 TYR B CB 2319 C CG . TYR B 89 ? 0.3906 0.3660 0.3425 0.0117 -0.0137 0.0089 88 TYR B CG 2320 C CD1 . TYR B 89 ? 0.3307 0.3146 0.2839 0.0097 -0.0128 0.0106 88 TYR B CD1 2321 C CD2 . TYR B 89 ? 0.4804 0.4451 0.4273 0.0138 -0.0170 0.0110 88 TYR B CD2 2322 C CE1 . TYR B 89 ? 0.3387 0.3208 0.2887 0.0098 -0.0152 0.0144 88 TYR B CE1 2323 C CE2 . TYR B 89 ? 0.4424 0.4050 0.3859 0.0139 -0.0195 0.0148 88 TYR B CE2 2324 C CZ . TYR B 89 ? 0.4298 0.4012 0.3750 0.0119 -0.0185 0.0164 88 TYR B CZ 2325 O OH . TYR B 89 ? 0.3885 0.3580 0.3304 0.0120 -0.0208 0.0201 88 TYR B OH 2326 N N . ILE B 90 ? 0.3606 0.3400 0.3245 0.0098 -0.0098 -0.0023 89 ILE B N 2327 C CA . ILE B 90 ? 0.3756 0.3541 0.3421 0.0104 -0.0076 -0.0059 89 ILE B CA 2328 C C . ILE B 90 ? 0.3557 0.3215 0.3167 0.0147 -0.0079 -0.0056 89 ILE B C 2329 O O . ILE B 90 ? 0.3651 0.3220 0.3221 0.0163 -0.0112 -0.0038 89 ILE B O 2330 C CB . ILE B 90 ? 0.4492 0.4304 0.4200 0.0082 -0.0090 -0.0076 89 ILE B CB 2331 C CG1 . ILE B 90 ? 0.4225 0.4165 0.3989 0.0040 -0.0084 -0.0080 89 ILE B CG1 2332 C CG2 . ILE B 90 ? 0.4367 0.4163 0.4100 0.0090 -0.0067 -0.0112 89 ILE B CG2 2333 C CD1 . ILE B 90 ? 0.5089 0.5118 0.4896 0.0025 -0.0042 -0.0107 89 ILE B CD1 2334 N N . CYS B 91 ? 0.4007 0.3654 0.3613 0.0165 -0.0046 -0.0075 90 CYS B N 2335 C CA . CYS B 91 ? 0.3819 0.3354 0.3385 0.0203 -0.0044 -0.0082 90 CYS B CA 2336 C C . CYS B 91 ? 0.3907 0.3442 0.3512 0.0199 -0.0036 -0.0115 90 CYS B C 2337 O O . CYS B 91 ? 0.4271 0.3892 0.3929 0.0178 -0.0007 -0.0144 90 CYS B O 2338 C CB . CYS B 91 ? 0.2793 0.2308 0.2335 0.0227 -0.0012 -0.0086 90 CYS B CB 2339 S SG . CYS B 91 ? 0.3611 0.2974 0.3093 0.0277 -0.0016 -0.0086 90 CYS B SG 2340 N N . LYS B 92 ? 0.3431 0.2871 0.3009 0.0218 -0.0061 -0.0112 91 LYS B N 2341 C CA . LYS B 92 ? 0.4298 0.3738 0.3912 0.0212 -0.0059 -0.0140 91 LYS B CA 2342 C C . LYS B 92 ? 0.4628 0.3953 0.4203 0.0251 -0.0058 -0.0148 91 LYS B C 2343 O O . LYS B 92 ? 0.3962 0.3232 0.3500 0.0261 -0.0079 -0.0116 91 LYS B O 2344 C CB . LYS B 92 ? 0.3995 0.3448 0.3626 0.0189 -0.0095 -0.0129 91 LYS B CB 2345 C CG . LYS B 92 ? 0.5548 0.5040 0.5234 0.0170 -0.0090 -0.0157 91 LYS B CG 2346 C CD . LYS B 92 ? 0.5625 0.5127 0.5322 0.0148 -0.0129 -0.0140 91 LYS B CD 2347 C CE . LYS B 92 ? 0.7427 0.6983 0.7185 0.0123 -0.0124 -0.0166 91 LYS B CE 2348 N NZ . LYS B 92 ? 0.7047 0.6617 0.6817 0.0101 -0.0162 -0.0148 91 LYS B NZ 2349 N N . ALA B 93 ? 0.5200 0.4558 0.4818 0.0248 -0.0027 -0.0176 92 ALA B N 2350 C CA . ALA B 93 ? 0.4897 0.4258 0.4549 0.0242 -0.0021 -0.0165 92 ALA B CA 2351 C C . ALA B 93 ? 0.4552 0.3924 0.4245 0.0229 -0.0025 -0.0183 92 ALA B C 2352 O O . ALA B 93 ? 0.4328 0.3745 0.4057 0.0219 -0.0004 -0.0217 92 ALA B O 2353 C CB . ALA B 93 ? 0.4589 0.3996 0.4277 0.0240 0.0017 -0.0174 92 ALA B CB 2354 N N . VAL B 94 ? 0.4672 0.4009 0.4357 0.0227 -0.0051 -0.0162 93 VAL B N 2355 C CA . VAL B 94 ? 0.5325 0.4673 0.5051 0.0215 -0.0050 -0.0175 93 VAL B CA 2356 C C . VAL B 94 ? 0.4712 0.4083 0.4476 0.0212 -0.0025 -0.0172 93 VAL B C 2357 O O . VAL B 94 ? 0.4433 0.3790 0.4179 0.0218 -0.0030 -0.0149 93 VAL B O 2358 C CB . VAL B 94 ? 0.4704 0.4011 0.4406 0.0213 -0.0091 -0.0156 93 VAL B CB 2359 C CG1 . VAL B 94 ? 0.3974 0.3294 0.3719 0.0201 -0.0088 -0.0170 93 VAL B CG1 2360 C CG2 . VAL B 94 ? 0.4684 0.3970 0.4357 0.0213 -0.0121 -0.0159 93 VAL B CG2 2361 N N . THR B 95 ? 0.4963 0.4371 0.4780 0.0201 0.0001 -0.0196 94 THR B N 2362 C CA . THR B 95 ? 0.5204 0.4641 0.5066 0.0195 0.0026 -0.0198 94 THR B CA 2363 C C . THR B 95 ? 0.4436 0.3869 0.4321 0.0188 0.0028 -0.0205 94 THR B C 2364 O O . THR B 95 ? 0.4304 0.3736 0.4198 0.0179 0.0025 -0.0214 94 THR B O 2365 C CB . THR B 95 ? 0.5042 0.4531 0.4941 0.0189 0.0058 -0.0222 94 THR B CB 2366 O OG1 . THR B 95 ? 0.4269 0.3787 0.4187 0.0178 0.0077 -0.0251 94 THR B OG1 2367 C CG2 . THR B 95 ? 0.4812 0.4295 0.4673 0.0201 0.0053 -0.0210 94 THR B CG2 2368 N N . PHE B 96 ? 0.3728 0.3146 0.3603 0.0199 0.0027 -0.0200 95 PHE B N 2369 C CA . PHE B 96 ? 0.3972 0.3387 0.3869 0.0195 0.0031 -0.0207 95 PHE B CA 2370 C C . PHE B 96 ? 0.3642 0.3091 0.3580 0.0191 0.0061 -0.0227 95 PHE B C 2371 O O . PHE B 96 ? 0.5141 0.4586 0.5062 0.0203 0.0060 -0.0222 95 PHE B O 2372 C CB . PHE B 96 ? 0.3741 0.3108 0.3589 0.0209 0.0001 -0.0183 95 PHE B CB 2373 C CG . PHE B 96 ? 0.4082 0.3444 0.3950 0.0206 0.0003 -0.0189 95 PHE B CG 2374 C CD1 . PHE B 96 ? 0.3768 0.3122 0.3644 0.0198 -0.0008 -0.0188 95 PHE B CD1 2375 C CD2 . PHE B 96 ? 0.3032 0.2399 0.2910 0.0212 0.0018 -0.0195 95 PHE B CD2 2376 C CE1 . PHE B 96 ? 0.3509 0.2858 0.3402 0.0196 -0.0006 -0.0192 95 PHE B CE1 2377 C CE2 . PHE B 96 ? 0.3299 0.2662 0.3196 0.0209 0.0021 -0.0200 95 PHE B CE2 2378 C CZ . PHE B 96 ? 0.4302 0.3655 0.4205 0.0201 0.0010 -0.0198 95 PHE B CZ 2379 N N . PRO B 97 ? 0.4059 0.3541 0.4037 0.0174 0.0085 -0.0243 96 PRO B N 2380 C CA . PRO B 97 ? 0.4512 0.3990 0.4484 0.0159 0.0092 -0.0242 96 PRO B CA 2381 C C . PRO B 97 ? 0.4070 0.3559 0.4008 0.0145 0.0112 -0.0243 96 PRO B C 2382 O O . PRO B 97 ? 0.4631 0.4099 0.4540 0.0144 0.0097 -0.0246 96 PRO B O 2383 C CB . PRO B 97 ? 0.3958 0.3434 0.3922 0.0154 0.0115 -0.0240 96 PRO B CB 2384 C CG . PRO B 97 ? 0.2858 0.2363 0.2833 0.0154 0.0140 -0.0243 96 PRO B CG 2385 C CD . PRO B 97 ? 0.3686 0.3196 0.3691 0.0172 0.0100 -0.0252 96 PRO B CD 2386 N N . LEU B 98 ? 0.4542 0.4053 0.4466 0.0143 0.0128 -0.0243 97 LEU B N 2387 C CA . LEU B 98 ? 0.3970 0.3482 0.3825 0.0167 0.0103 -0.0258 97 LEU B CA 2388 C C . LEU B 98 ? 0.5425 0.4937 0.5311 0.0157 0.0089 -0.0281 97 LEU B C 2389 O O . LEU B 98 ? 0.5955 0.5532 0.5885 0.0148 0.0077 -0.0313 97 LEU B O 2390 C CB . LEU B 98 ? 0.5894 0.5455 0.5741 0.0184 0.0103 -0.0264 97 LEU B CB 2391 C CG . LEU B 98 ? 0.5941 0.5537 0.5804 0.0196 0.0106 -0.0269 97 LEU B CG 2392 C CD1 . LEU B 98 ? 0.6759 0.6415 0.6646 0.0195 0.0127 -0.0283 97 LEU B CD1 2393 C CD2 . LEU B 98 ? 0.4934 0.4550 0.4838 0.0185 0.0116 -0.0286 97 LEU B CD2 2394 N N . GLY B 99 ? 0.5798 0.5287 0.5708 0.0156 0.0074 -0.0272 98 GLY B N 2395 C CA . GLY B 99 ? 0.5542 0.5019 0.5434 0.0162 0.0029 -0.0276 98 GLY B CA 2396 C C . GLY B 99 ? 0.5117 0.4604 0.4984 0.0173 0.0026 -0.0277 98 GLY B C 2397 O O . GLY B 99 ? 0.4975 0.4464 0.4838 0.0180 0.0043 -0.0264 98 GLY B O 2398 N N . ASN B 100 ? 0.4731 0.4233 0.4590 0.0171 0.0000 -0.0296 99 ASN B N 2399 C CA . ASN B 100 ? 0.6301 0.5814 0.6127 0.0174 -0.0007 -0.0279 99 ASN B CA 2400 C C . ASN B 100 ? 0.7317 0.6922 0.7173 0.0160 0.0036 -0.0297 99 ASN B C 2401 O O . ASN B 100 ? 0.6903 0.6586 0.6816 0.0139 0.0065 -0.0325 99 ASN B O 2402 C CB . ASN B 100 ? 0.6147 0.5696 0.5978 0.0147 -0.0042 -0.0254 99 ASN B CB 2403 C CG . ASN B 100 ? 0.7551 0.7207 0.7451 0.0107 -0.0031 -0.0271 99 ASN B CG 2404 O OD1 . ASN B 100 ? 0.8859 0.8533 0.8800 0.0101 -0.0013 -0.0298 99 ASN B OD1 2405 N ND2 . ASN B 100 ? 0.8894 0.8624 0.8809 0.0078 -0.0042 -0.0256 99 ASN B ND2 2406 N N . ALA B 101 ? 0.6302 0.5894 0.6118 0.0174 0.0039 -0.0279 100 ALA B N 2407 C CA . ALA B 101 ? 0.5285 0.4963 0.5122 0.0161 0.0073 -0.0288 100 ALA B CA 2408 C C . ALA B 101 ? 0.5679 0.5355 0.5476 0.0161 0.0053 -0.0254 100 ALA B C 2409 O O . ALA B 101 ? 0.5371 0.4960 0.5116 0.0181 0.0019 -0.0227 100 ALA B O 2410 C CB . ALA B 101 ? 0.4480 0.4131 0.4308 0.0188 0.0111 -0.0310 100 ALA B CB 2411 N N . GLN B 102 ? 0.4922 0.4696 0.4744 0.0137 0.0072 -0.0254 101 GLN B N 2412 C CA . GLN B 102 ? 0.4918 0.4699 0.4708 0.0133 0.0052 -0.0220 101 GLN B CA 2413 C C . GLN B 102 ? 0.4953 0.4825 0.4761 0.0118 0.0083 -0.0224 101 GLN B C 2414 O O . GLN B 102 ? 0.4265 0.4210 0.4118 0.0103 0.0119 -0.0253 101 GLN B O 2415 C CB . GLN B 102 ? 0.3241 0.3052 0.3047 0.0106 0.0017 -0.0203 101 GLN B CB 2416 C CG . GLN B 102 ? 0.4143 0.4079 0.4014 0.0064 0.0031 -0.0219 101 GLN B CG 2417 C CD . GLN B 102 ? 0.4311 0.4267 0.4197 0.0040 -0.0005 -0.0203 101 GLN B CD 2418 O OE1 . GLN B 102 ? 0.5164 0.5206 0.5075 0.0010 -0.0008 -0.0194 101 GLN B OE1 2419 N NE2 . GLN B 102 ? 0.4273 0.4151 0.4144 0.0052 -0.0033 -0.0199 101 GLN B NE2 2420 N N . SER B 103 ? 0.4055 0.3920 0.3827 0.0123 0.0070 -0.0193 102 SER B N 2421 C CA . SER B 103 ? 0.4235 0.4192 0.4022 0.0104 0.0091 -0.0188 102 SER B CA 2422 C C . SER B 103 ? 0.4462 0.4415 0.4218 0.0099 0.0061 -0.0148 102 SER B C 2423 O O . SER B 103 ? 0.3852 0.3709 0.3557 0.0122 0.0031 -0.0124 102 SER B O 2424 C CB . SER B 103 ? 0.3831 0.3770 0.3598 0.0128 0.0125 -0.0196 102 SER B CB 2425 O OG . SER B 103 ? 0.5153 0.5105 0.4953 0.0131 0.0157 -0.0234 102 SER B OG 2426 N N . SER B 104 ? 0.4291 0.4349 0.4076 0.0068 0.0069 -0.0143 103 SER B N 2427 C CA . SER B 104 ? 0.4299 0.4375 0.4067 0.0056 0.0041 -0.0108 103 SER B CA 2428 C C . SER B 104 ? 0.4712 0.4795 0.4449 0.0066 0.0054 -0.0086 103 SER B C 2429 O O . SER B 104 ? 0.4578 0.4702 0.4328 0.0068 0.0089 -0.0102 103 SER B O 2430 C CB . SER B 104 ? 0.4114 0.4305 0.3939 0.0011 0.0038 -0.0114 103 SER B CB 2431 O OG . SER B 104 ? 0.4505 0.4798 0.4371 -0.0010 0.0075 -0.0133 103 SER B OG 2432 N N . THR B 105 ? 0.4698 0.4742 0.4394 0.0074 0.0025 -0.0049 104 THR B N 2433 C CA . THR B 105 ? 0.3972 0.4025 0.3638 0.0081 0.0031 -0.0022 104 THR B CA 2434 C C . THR B 105 ? 0.4393 0.4496 0.4064 0.0057 0.0004 0.0007 104 THR B C 2435 O O . THR B 105 ? 0.4700 0.4745 0.4349 0.0062 -0.0031 0.0025 104 THR B O 2436 C CB . THR B 105 ? 0.3203 0.3131 0.2802 0.0124 0.0022 -0.0002 104 THR B CB 2437 O OG1 . THR B 105 ? 0.4738 0.4631 0.4331 0.0147 0.0053 -0.0025 104 THR B OG1 2438 C CG2 . THR B 105 ? 0.4335 0.4268 0.3901 0.0128 0.0019 0.0034 104 THR B CG2 2439 N N . THR B 106 ? 0.3998 0.4205 0.3697 0.0031 0.0020 0.0012 105 THR B N 2440 C CA . THR B 106 ? 0.4333 0.4591 0.4037 0.0009 -0.0003 0.0041 105 THR B CA 2441 C C . THR B 106 ? 0.4085 0.4301 0.3737 0.0029 -0.0008 0.0078 105 THR B C 2442 O O . THR B 106 ? 0.4636 0.4850 0.4274 0.0044 0.0018 0.0078 105 THR B O 2443 C CB . THR B 106 ? 0.4303 0.4703 0.4067 -0.0033 0.0015 0.0028 105 THR B CB 2444 O OG1 . THR B 106 ? 0.4910 0.5347 0.4722 -0.0050 0.0025 -0.0008 105 THR B OG1 2445 C CG2 . THR B 106 ? 0.2417 0.2865 0.2189 -0.0056 -0.0012 0.0055 105 THR B CG2 2446 N N . VAL B 107 ? 0.3953 0.4136 0.3579 0.0030 -0.0042 0.0110 106 VAL B N 2447 C CA . VAL B 107 ? 0.3517 0.3653 0.3092 0.0050 -0.0049 0.0148 106 VAL B CA 2448 C C . VAL B 107 ? 0.3627 0.3850 0.3219 0.0022 -0.0059 0.0173 106 VAL B C 2449 O O . VAL B 107 ? 0.3236 0.3494 0.2852 0.0000 -0.0082 0.0177 106 VAL B O 2450 C CB . VAL B 107 ? 0.3768 0.3769 0.3285 0.0082 -0.0079 0.0167 106 VAL B CB 2451 C CG1 . VAL B 107 ? 0.3139 0.3106 0.2610 0.0095 -0.0091 0.0209 106 VAL B CG1 2452 C CG2 . VAL B 107 ? 0.3462 0.3372 0.2952 0.0115 -0.0065 0.0148 106 VAL B CG2 2453 N N . THR B 108 ? 0.3543 0.3803 0.3126 0.0023 -0.0039 0.0191 107 THR B N 2454 C CA . THR B 108 ? 0.3371 0.3708 0.2965 0.0001 -0.0046 0.0220 107 THR B CA 2455 C C . THR B 108 ? 0.3430 0.3685 0.2964 0.0028 -0.0061 0.0261 107 THR B C 2456 O O . THR B 108 ? 0.2981 0.3176 0.2478 0.0055 -0.0045 0.0267 107 THR B O 2457 C CB . THR B 108 ? 0.3727 0.4178 0.3360 -0.0021 -0.0012 0.0209 107 THR B CB 2458 O OG1 . THR B 108 ? 0.3200 0.3729 0.2890 -0.0048 0.0001 0.0171 107 THR B OG1 2459 C CG2 . THR B 108 ? 0.2680 0.3208 0.2320 -0.0041 -0.0017 0.0242 107 THR B CG2 2460 N N . VAL B 109 ? 0.2815 0.3064 0.2337 0.0020 -0.0092 0.0288 108 VAL B N 2461 C CA . VAL B 109 ? 0.2628 0.2788 0.2105 0.0043 -0.0104 0.0318 108 VAL B CA 2462 C C . VAL B 109 ? 0.3107 0.3332 0.2614 0.0027 -0.0087 0.0325 108 VAL B C 2463 O O . VAL B 109 ? 0.3258 0.3585 0.2811 -0.0003 -0.0087 0.0325 108 VAL B O 2464 C CB . VAL B 109 ? 0.3006 0.3098 0.2470 0.0045 -0.0140 0.0325 108 VAL B CB 2465 C CG1 . VAL B 109 ? 0.3051 0.3050 0.2483 0.0062 -0.0146 0.0335 108 VAL B CG1 2466 C CG2 . VAL B 109 ? 0.2472 0.2480 0.1903 0.0066 -0.0158 0.0318 108 VAL B CG2 2467 N N . LEU B 110 ? 0.3143 0.3306 0.2624 0.0046 -0.0072 0.0330 109 LEU B N 2468 C CA . LEU B 110 ? 0.2922 0.3128 0.2427 0.0036 -0.0058 0.0339 109 LEU B CA 2469 C C . LEU B 110 ? 0.2720 0.2822 0.2190 0.0050 -0.0075 0.0350 109 LEU B C 2470 O O . LEU B 110 ? 0.2712 0.2701 0.2137 0.0066 -0.0093 0.0347 109 LEU B O 2471 C CB . LEU B 110 ? 0.3199 0.3423 0.2706 0.0043 -0.0026 0.0332 109 LEU B CB 2472 C CG . LEU B 110 ? 0.3170 0.3472 0.2699 0.0036 -0.0005 0.0314 109 LEU B CG 2473 C CD1 . LEU B 110 ? 0.3547 0.3836 0.3069 0.0050 0.0025 0.0305 109 LEU B CD1 2474 C CD2 . LEU B 110 ? 0.3218 0.3660 0.2808 -0.0002 0.0001 0.0306 109 LEU B CD2 2475 N N . VAL B 111 ? 0.3067 0.3214 0.2562 0.0038 -0.0071 0.0359 110 VAL B N 2476 C CA . VAL B 111 ? 0.2787 0.2851 0.2253 0.0048 -0.0083 0.0366 110 VAL B CA 2477 C C . VAL B 111 ? 0.2785 0.2869 0.2261 0.0046 -0.0062 0.0371 110 VAL B C 2478 O O . VAL B 111 ? 0.3386 0.3582 0.2912 0.0030 -0.0046 0.0375 110 VAL B O 2479 C CB . VAL B 111 ? 0.2987 0.3088 0.2475 0.0036 -0.0100 0.0373 110 VAL B CB 2480 C CG1 . VAL B 111 ? 0.3114 0.3131 0.2569 0.0048 -0.0109 0.0378 110 VAL B CG1 2481 C CG2 . VAL B 111 ? 0.2713 0.2804 0.2197 0.0035 -0.0121 0.0368 110 VAL B CG2 2482 N N . GLU B 112 ? 0.3252 0.3234 0.2685 0.0058 -0.0066 0.0370 111 GLU B N 2483 C CA . GLU B 112 ? 0.3055 0.3048 0.2496 0.0057 -0.0049 0.0374 111 GLU B CA 2484 C C . GLU B 112 ? 0.3698 0.3738 0.3164 0.0048 -0.0050 0.0385 111 GLU B C 2485 O O . GLU B 112 ? 0.3745 0.3748 0.3196 0.0051 -0.0069 0.0389 111 GLU B O 2486 C CB . GLU B 112 ? 0.3576 0.3469 0.2980 0.0062 -0.0058 0.0375 111 GLU B CB 2487 C CG . GLU B 112 ? 0.5028 0.4886 0.4426 0.0064 -0.0059 0.0366 111 GLU B CG 2488 C CD . GLU B 112 ? 0.6595 0.6419 0.6000 0.0075 -0.0058 0.0376 111 GLU B CD 2489 O OE1 . GLU B 112 ? 0.7055 0.6856 0.6456 0.0077 -0.0067 0.0390 111 GLU B OE1 2490 O OE2 . GLU B 112 ? 0.6078 0.5902 0.5495 0.0087 -0.0042 0.0369 111 GLU B OE2 2491 N N . PRO B 113 ? 0.3336 0.3467 0.2847 0.0039 -0.0031 0.0391 112 PRO B N 2492 C CA . PRO B 113 ? 0.3206 0.3389 0.2747 0.0029 -0.0033 0.0406 112 PRO B CA 2493 C C . PRO B 113 ? 0.3273 0.3394 0.2789 0.0043 -0.0035 0.0419 112 PRO B C 2494 O O . PRO B 113 ? 0.3309 0.3368 0.2795 0.0055 -0.0030 0.0417 112 PRO B O 2495 C CB . PRO B 113 ? 0.3037 0.3335 0.2635 0.0014 -0.0014 0.0407 112 PRO B CB 2496 C CG . PRO B 113 ? 0.3210 0.3482 0.2791 0.0024 0.0003 0.0397 112 PRO B CG 2497 C CD . PRO B 113 ? 0.3140 0.3342 0.2682 0.0035 -0.0008 0.0388 112 PRO B CD 2498 N N . THR B 114 ? 0.3198 0.3338 0.2727 0.0039 -0.0044 0.0433 113 THR B N 2499 C CA . THR B 114 ? 0.2840 0.2940 0.2353 0.0048 -0.0044 0.0447 113 THR B CA 2500 C C . THR B 114 ? 0.3361 0.3556 0.2926 0.0039 -0.0027 0.0460 113 THR B C 2501 O O . THR B 114 ? 0.3359 0.3637 0.2968 0.0023 -0.0030 0.0468 113 THR B O 2502 C CB . THR B 114 ? 0.3601 0.3665 0.3098 0.0050 -0.0063 0.0454 113 THR B CB 2503 O OG1 . THR B 114 ? 0.4088 0.4075 0.3544 0.0057 -0.0080 0.0441 113 THR B OG1 2504 C CG2 . THR B 114 ? 0.3051 0.3063 0.2526 0.0060 -0.0063 0.0467 113 THR B CG2 2505 N N . VAL B 115 ? 0.2837 0.3022 0.2398 0.0048 -0.0012 0.0463 114 VAL B N 2506 C CA . VAL B 115 ? 0.3001 0.3275 0.2611 0.0040 0.0003 0.0473 114 VAL B CA 2507 C C . VAL B 115 ? 0.4240 0.4497 0.3847 0.0048 0.0004 0.0491 114 VAL B C 2508 O O . VAL B 115 ? 0.4664 0.4831 0.4227 0.0063 0.0001 0.0492 114 VAL B O 2509 C CB . VAL B 115 ? 0.3172 0.3454 0.2784 0.0046 0.0020 0.0464 114 VAL B CB 2510 C CG1 . VAL B 115 ? 0.3223 0.3589 0.2882 0.0041 0.0034 0.0474 114 VAL B CG1 2511 C CG2 . VAL B 115 ? 0.3867 0.4175 0.3486 0.0037 0.0021 0.0446 114 VAL B CG2 2512 N N . SER B 116 ? 0.3887 0.4236 0.3545 0.0035 0.0007 0.0504 115 SER B N 2513 C CA . SER B 116 ? 0.3683 0.4034 0.3349 0.0041 0.0012 0.0522 115 SER B CA 2514 C C . SER B 116 ? 0.3848 0.4312 0.3575 0.0029 0.0022 0.0532 115 SER B C 2515 O O . SER B 116 ? 0.3220 0.3771 0.2990 0.0011 0.0019 0.0528 115 SER B O 2516 C CB . SER B 116 ? 0.3257 0.3590 0.2916 0.0038 -0.0003 0.0532 115 SER B CB 2517 O OG . SER B 116 ? 0.4097 0.4513 0.3799 0.0018 -0.0011 0.0534 115 SER B OG 2518 N N . LEU B 117 ? 0.4258 0.4719 0.3990 0.0040 0.0033 0.0543 116 LEU B N 2519 C CA . LEU B 117 ? 0.4292 0.4855 0.4081 0.0030 0.0039 0.0555 116 LEU B CA 2520 C C . LEU B 117 ? 0.4525 0.5101 0.4327 0.0031 0.0037 0.0575 116 LEU B C 2521 O O . LEU B 117 ? 0.4468 0.4966 0.4233 0.0047 0.0040 0.0581 116 LEU B O 2522 C CB . LEU B 117 ? 0.4104 0.4666 0.3894 0.0041 0.0055 0.0552 116 LEU B CB 2523 C CG . LEU B 117 ? 0.4052 0.4720 0.3900 0.0032 0.0060 0.0563 116 LEU B CG 2524 C CD1 . LEU B 117 ? 0.3518 0.4287 0.3412 0.0010 0.0052 0.0555 116 LEU B CD1 2525 C CD2 . LEU B 117 ? 0.3842 0.4488 0.3681 0.0047 0.0075 0.0561 116 LEU B CD2 2526 N N . ILE B 118 ? 0.4578 0.5253 0.4435 0.0013 0.0030 0.0585 117 ILE B N 2527 C CA . ILE B 118 ? 0.4405 0.5100 0.4279 0.0012 0.0027 0.0604 117 ILE B CA 2528 C C . ILE B 118 ? 0.4766 0.5572 0.4702 0.0002 0.0029 0.0617 117 ILE B C 2529 O O . ILE B 118 ? 0.4350 0.5231 0.4322 -0.0011 0.0028 0.0610 117 ILE B O 2530 C CB . ILE B 118 ? 0.4063 0.4759 0.3937 0.0000 0.0012 0.0604 117 ILE B CB 2531 C CG1 . ILE B 118 ? 0.4318 0.4927 0.4149 0.0014 0.0010 0.0612 117 ILE B CG1 2532 C CG2 . ILE B 118 ? 0.4117 0.4931 0.4055 -0.0023 0.0004 0.0614 117 ILE B CG2 2533 C CD1 . ILE B 118 ? 0.4498 0.4988 0.4263 0.0035 0.0015 0.0601 117 ILE B CD1 2534 N N . LYS B 119 ? 0.5195 0.6008 0.5143 0.0007 0.0032 0.0635 118 LYS B N 2535 C CA . LYS B 119 ? 0.5246 0.6162 0.5252 -0.0001 0.0032 0.0650 118 LYS B CA 2536 C C . LYS B 119 ? 0.5184 0.6190 0.5237 -0.0024 0.0016 0.0655 118 LYS B C 2537 O O . LYS B 119 ? 0.4866 0.5846 0.4906 -0.0029 0.0009 0.0654 118 LYS B O 2538 C CB . LYS B 119 ? 0.5653 0.6546 0.5656 0.0014 0.0041 0.0667 118 LYS B CB 2539 C CG . LYS B 119 ? 0.7089 0.7915 0.7058 0.0034 0.0056 0.0664 118 LYS B CG 2540 C CD . LYS B 119 ? 0.7086 0.7890 0.7053 0.0049 0.0065 0.0681 118 LYS B CD 2541 C CE . LYS B 119 ? 0.7198 0.7936 0.7133 0.0069 0.0081 0.0677 118 LYS B CE 2542 N NZ . LYS B 119 ? 0.8598 0.9312 0.8530 0.0083 0.0090 0.0693 118 LYS B NZ 2543 N N . GLY B 120 ? 0.5470 0.6583 0.5578 -0.0038 0.0010 0.0660 119 GLY B N 2544 C CA . GLY B 120 ? 0.5241 0.6449 0.5399 -0.0059 -0.0006 0.0666 119 GLY B CA 2545 C C . GLY B 120 ? 0.6518 0.7726 0.6685 -0.0058 -0.0007 0.0685 119 GLY B C 2546 O O . GLY B 120 ? 0.5829 0.6982 0.5974 -0.0040 0.0004 0.0696 119 GLY B O 2547 N N . PRO B 121 ? 0.6759 0.8029 0.6960 -0.0077 -0.0021 0.0688 120 PRO B N 2548 C CA . PRO B 121 ? 0.7203 0.8471 0.7412 -0.0076 -0.0023 0.0704 120 PRO B CA 2549 C C . PRO B 121 ? 0.8446 0.9786 0.8699 -0.0075 -0.0024 0.0725 120 PRO B C 2550 O O . PRO B 121 ? 0.7663 0.8978 0.7911 -0.0066 -0.0019 0.0740 120 PRO B O 2551 C CB . PRO B 121 ? 0.5858 0.7174 0.6090 -0.0098 -0.0038 0.0699 120 PRO B CB 2552 C CG . PRO B 121 ? 0.5985 0.7379 0.6249 -0.0114 -0.0047 0.0687 120 PRO B CG 2553 C CD . PRO B 121 ? 0.5759 0.7098 0.5988 -0.0099 -0.0035 0.0675 120 PRO B CD 2554 N N . ASP B 122 ? 0.8574 1.0000 0.8866 -0.0083 -0.0031 0.0726 121 ASP B N 2555 C CA . ASP B 122 ? 0.8131 0.9631 0.8466 -0.0082 -0.0036 0.0745 121 ASP B CA 2556 C C . ASP B 122 ? 0.8280 0.9755 0.8601 -0.0065 -0.0023 0.0748 121 ASP B C 2557 O O . ASP B 122 ? 0.8590 1.0030 0.8886 -0.0060 -0.0017 0.0733 121 ASP B O 2558 C CB . ASP B 122 ? 0.7743 0.9295 0.8089 -0.0103 -0.0050 0.0730 121 ASP B CB 2559 C CG . ASP B 122 ? 0.8584 1.0131 0.8926 -0.0119 -0.0058 0.0721 121 ASP B CG 2560 O OD1 . ASP B 122 ? 0.8078 0.9617 0.8431 -0.0114 -0.0056 0.0737 121 ASP B OD1 2561 O OD2 . ASP B 122 ? 0.9380 1.0931 0.9708 -0.0134 -0.0066 0.0698 121 ASP B OD2 2562 N N . SER B 123 ? 0.8703 1.0195 0.9042 -0.0055 -0.0019 0.0768 122 SER B N 2563 C CA . SER B 123 ? 0.7701 0.9180 0.8035 -0.0039 -0.0008 0.0774 122 SER B CA 2564 C C . SER B 123 ? 0.7599 0.9171 0.7968 -0.0049 -0.0022 0.0773 122 SER B C 2565 O O . SER B 123 ? 0.7559 0.9160 0.7930 -0.0068 -0.0035 0.0763 122 SER B O 2566 C CB . SER B 123 ? 0.7522 0.8998 0.7866 -0.0026 0.0000 0.0796 122 SER B CB 2567 O OG . SER B 123 ? 0.7121 0.8699 0.7519 -0.0040 -0.0018 0.0811 122 SER B OG 2568 N N . LEU B 124 ? 0.7717 0.9262 0.8068 -0.0039 -0.0013 0.0766 123 LEU B N 2569 C CA . LEU B 124 ? 0.7336 0.8933 0.7695 -0.0049 -0.0024 0.0757 123 LEU B CA 2570 C C . LEU B 124 ? 0.9002 1.0626 0.9374 -0.0045 -0.0024 0.0769 123 LEU B C 2571 O O . LEU B 124 ? 0.9780 1.1404 1.0158 -0.0029 -0.0015 0.0781 123 LEU B O 2572 C CB . LEU B 124 ? 0.7190 0.8749 0.7526 -0.0040 -0.0015 0.0743 123 LEU B CB 2573 C CG . LEU B 124 ? 0.8407 0.9881 0.8701 -0.0038 -0.0004 0.0724 123 LEU B CG 2574 C CD1 . LEU B 124 ? 0.7417 0.8821 0.7673 -0.0023 0.0012 0.0710 123 LEU B CD1 2575 C CD2 . LEU B 124 ? 0.7396 0.8929 0.7708 -0.0061 -0.0024 0.0711 123 LEU B CD2 2576 N N . ILE B 125 ? 0.9839 1.1486 1.0211 -0.0060 -0.0034 0.0767 124 ILE B N 2577 C CA . ILE B 125 ? 0.8782 1.0456 0.9166 -0.0058 -0.0035 0.0780 124 ILE B CA 2578 C C . ILE B 125 ? 0.7999 0.9691 0.8369 -0.0067 -0.0040 0.0766 124 ILE B C 2579 O O . ILE B 125 ? 0.7427 0.9124 0.7779 -0.0085 -0.0050 0.0744 124 ILE B O 2580 C CB . ILE B 125 ? 0.9170 1.0861 0.9560 -0.0070 -0.0043 0.0783 124 ILE B CB 2581 C CG1 . ILE B 125 ? 0.9510 1.1185 0.9913 -0.0062 -0.0037 0.0798 124 ILE B CG1 2582 C CG2 . ILE B 125 ? 0.9592 1.1312 0.9990 -0.0070 -0.0045 0.0794 124 ILE B CG2 2583 C CD1 . ILE B 125 ? 1.0565 1.2249 1.0992 -0.0045 -0.0028 0.0827 124 ILE B CD1 2584 N N . ASP B 126 ? 0.8393 1.0097 0.8773 -0.0054 -0.0034 0.0780 125 ASP B N 2585 C CA . ASP B 126 ? 0.7500 0.9225 0.7868 -0.0062 -0.0039 0.0770 125 ASP B CA 2586 C C . ASP B 126 ? 0.7486 0.9240 0.7847 -0.0082 -0.0053 0.0762 125 ASP B C 2587 O O . ASP B 126 ? 0.7484 0.9249 0.7856 -0.0084 -0.0055 0.0773 125 ASP B O 2588 C CB . ASP B 126 ? 0.6707 0.8438 0.7089 -0.0044 -0.0030 0.0789 125 ASP B CB 2589 C CG . ASP B 126 ? 0.7026 0.8778 0.7396 -0.0050 -0.0034 0.0780 125 ASP B CG 2590 O OD1 . ASP B 126 ? 0.7778 0.9538 0.8128 -0.0068 -0.0043 0.0759 125 ASP B OD1 2591 O OD2 . ASP B 126 ? 0.6947 0.8706 0.7328 -0.0036 -0.0027 0.0795 125 ASP B OD2 2592 N N . GLY B 127 ? 0.7267 0.9034 0.7609 -0.0096 -0.0060 0.0743 126 GLY B N 2593 C CA . GLY B 127 ? 0.7075 0.8867 0.7405 -0.0116 -0.0073 0.0732 126 GLY B CA 2594 C C . GLY B 127 ? 0.7098 0.8877 0.7418 -0.0128 -0.0079 0.0718 126 GLY B C 2595 O O . GLY B 127 ? 0.6987 0.8784 0.7297 -0.0143 -0.0089 0.0708 126 GLY B O 2596 N N A GLY B 128 ? 0.7116 0.8865 0.7440 -0.0122 -0.0074 0.0716 127 GLY B N 2597 N N B GLY B 128 ? 0.7146 0.8895 0.7471 -0.0122 -0.0074 0.0716 127 GLY B N 2598 C CA A GLY B 128 ? 0.6904 0.8640 0.7222 -0.0133 -0.0079 0.0704 127 GLY B CA 2599 C CA B GLY B 128 ? 0.6883 0.8618 0.7201 -0.0132 -0.0079 0.0704 127 GLY B CA 2600 C C A GLY B 128 ? 0.6887 0.8616 0.7180 -0.0147 -0.0085 0.0677 127 GLY B C 2601 C C B GLY B 128 ? 0.6929 0.8653 0.7222 -0.0146 -0.0084 0.0677 127 GLY B C 2602 O O A GLY B 128 ? 0.6651 0.8386 0.6931 -0.0149 -0.0085 0.0667 127 GLY B O 2603 O O B GLY B 128 ? 0.6669 0.8396 0.6952 -0.0146 -0.0083 0.0668 127 GLY B O 2604 N N . ASN B 129 ? 0.6822 0.8537 0.7108 -0.0157 -0.0090 0.0665 128 ASN B N 2605 C CA . ASN B 129 ? 0.6488 0.8193 0.6751 -0.0170 -0.0095 0.0640 128 ASN B CA 2606 C C . ASN B 129 ? 0.5853 0.7528 0.6114 -0.0163 -0.0088 0.0633 128 ASN B C 2607 O O . ASN B 129 ? 0.5808 0.7469 0.6085 -0.0148 -0.0080 0.0649 128 ASN B O 2608 C CB . ASN B 129 ? 0.5921 0.7623 0.6179 -0.0182 -0.0103 0.0631 128 ASN B CB 2609 C CG . ASN B 129 ? 0.7076 0.8779 0.7354 -0.0175 -0.0102 0.0649 128 ASN B CG 2610 O OD1 . ASN B 129 ? 0.7619 0.9317 0.7916 -0.0162 -0.0094 0.0668 128 ASN B OD1 2611 N ND2 . ASN B 129 ? 0.6527 0.8238 0.6802 -0.0185 -0.0110 0.0645 128 ASN B ND2 2612 N N . GLU B 130 ? 0.5920 0.7588 0.6161 -0.0173 -0.0091 0.0611 129 GLU B N 2613 C CA . GLU B 130 ? 0.5922 0.7562 0.6158 -0.0168 -0.0085 0.0602 129 GLU B CA 2614 C C . GLU B 130 ? 0.6128 0.7743 0.6378 -0.0160 -0.0081 0.0612 129 GLU B C 2615 O O . GLU B 130 ? 0.5932 0.7542 0.6184 -0.0167 -0.0086 0.0610 129 GLU B O 2616 C CB . GLU B 130 ? 0.5887 0.7521 0.6099 -0.0183 -0.0091 0.0575 129 GLU B CB 2617 C CG . GLU B 130 ? 0.6345 0.7959 0.6548 -0.0178 -0.0085 0.0564 129 GLU B CG 2618 C CD . GLU B 130 ? 0.7257 0.8876 0.7436 -0.0193 -0.0089 0.0539 129 GLU B CD 2619 O OE1 . GLU B 130 ? 0.8568 1.0194 0.8734 -0.0206 -0.0097 0.0528 129 GLU B OE1 2620 O OE2 . GLU B 130 ? 0.7338 0.8954 0.7509 -0.0190 -0.0085 0.0530 129 GLU B OE2 2621 N N . THR B 131 ? 0.5980 0.7579 0.6240 -0.0144 -0.0071 0.0625 130 THR B N 2622 C CA . THR B 131 ? 0.5879 0.7456 0.6152 -0.0135 -0.0066 0.0638 130 THR B CA 2623 C C . THR B 131 ? 0.5479 0.7030 0.5744 -0.0129 -0.0060 0.0631 130 THR B C 2624 O O . THR B 131 ? 0.5343 0.6895 0.5599 -0.0125 -0.0057 0.0623 130 THR B O 2625 C CB . THR B 131 ? 0.4305 0.5889 0.4600 -0.0119 -0.0059 0.0667 130 THR B CB 2626 N N . VAL B 132 ? 0.4827 0.6356 0.5094 -0.0128 -0.0059 0.0633 131 VAL B N 2627 C CA . VAL B 132 ? 0.4894 0.6398 0.5156 -0.0120 -0.0053 0.0630 131 VAL B CA 2628 C C . VAL B 132 ? 0.4843 0.6321 0.5108 -0.0097 -0.0039 0.0652 131 VAL B C 2629 O O . VAL B 132 ? 0.4295 0.5739 0.4556 -0.0088 -0.0032 0.0666 131 VAL B O 2630 C CB . VAL B 132 ? 0.5038 0.6520 0.5295 -0.0129 -0.0056 0.0625 131 VAL B CB 2631 C CG1 . VAL B 132 ? 0.3455 0.4884 0.3691 -0.0118 -0.0046 0.0620 131 VAL B CG1 2632 C CG2 . VAL B 132 ? 0.4010 0.5495 0.4251 -0.0149 -0.0065 0.0598 131 VAL B CG2 2633 N N . ALA B 133 ? 0.4302 0.5742 0.4543 -0.0085 -0.0027 0.0643 132 ALA B N 2634 C CA . ALA B 133 ? 0.5289 0.6651 0.5501 -0.0061 -0.0006 0.0652 132 ALA B CA 2635 C C . ALA B 133 ? 0.5458 0.6705 0.5616 -0.0047 0.0009 0.0641 132 ALA B C 2636 O O . ALA B 133 ? 0.4787 0.5959 0.4916 -0.0029 0.0022 0.0649 132 ALA B O 2637 C CB . ALA B 133 ? 0.5057 0.6433 0.5270 -0.0053 -0.0001 0.0649 132 ALA B CB 2638 N N . ALA B 134 ? 0.5241 0.6471 0.5384 -0.0056 0.0005 0.0622 133 ALA B N 2639 C CA . ALA B 134 ? 0.4843 0.5965 0.4931 -0.0044 0.0016 0.0611 133 ALA B CA 2640 C C . ALA B 134 ? 0.4397 0.5530 0.4484 -0.0060 0.0006 0.0594 133 ALA B C 2641 O O . ALA B 134 ? 0.5241 0.6458 0.5363 -0.0079 -0.0006 0.0587 133 ALA B O 2642 C CB . ALA B 134 ? 0.4319 0.5369 0.4369 -0.0024 0.0032 0.0602 133 ALA B CB 2643 N N . VAL B 135 ? 0.4152 0.5195 0.4194 -0.0052 0.0009 0.0588 134 VAL B N 2644 C CA . VAL B 135 ? 0.4213 0.5250 0.4247 -0.0064 0.0001 0.0573 134 VAL B CA 2645 C C . VAL B 135 ? 0.3715 0.4643 0.3688 -0.0047 0.0010 0.0559 134 VAL B C 2646 O O . VAL B 135 ? 0.4106 0.4941 0.4035 -0.0029 0.0015 0.0564 134 VAL B O 2647 C CB . VAL B 135 ? 0.3907 0.4952 0.3950 -0.0074 -0.0011 0.0582 134 VAL B CB 2648 C CG1 . VAL B 135 ? 0.3440 0.4486 0.3478 -0.0089 -0.0020 0.0566 134 VAL B CG1 2649 C CG2 . VAL B 135 ? 0.4214 0.5364 0.4316 -0.0089 -0.0020 0.0597 134 VAL B CG2 2650 N N . CYS B 136 ? 0.3488 0.4426 0.3459 -0.0053 0.0011 0.0540 135 CYS B N 2651 C CA . CYS B 136 ? 0.3250 0.4092 0.3167 -0.0039 0.0018 0.0525 135 CYS B CA 2652 C C . CYS B 136 ? 0.4298 0.5128 0.4205 -0.0050 0.0006 0.0513 135 CYS B C 2653 O O . CYS B 136 ? 0.3314 0.4226 0.3261 -0.0072 -0.0001 0.0505 135 CYS B O 2654 C CB . CYS B 136 ? 0.3110 0.3963 0.3028 -0.0035 0.0029 0.0512 135 CYS B CB 2655 S SG . CYS B 136 ? 0.5054 0.5770 0.4899 -0.0009 0.0041 0.0499 135 CYS B SG 2656 N N . VAL B 137 ? 0.3141 0.3868 0.2995 -0.0036 0.0004 0.0511 136 VAL B N 2657 C CA . VAL B 137 ? 0.3077 0.3778 0.2914 -0.0043 -0.0008 0.0500 136 VAL B CA 2658 C C . VAL B 137 ? 0.2886 0.3495 0.2669 -0.0027 -0.0004 0.0484 136 VAL B C 2659 O O . VAL B 137 ? 0.3060 0.3586 0.2801 -0.0006 0.0003 0.0486 136 VAL B O 2660 C CB . VAL B 137 ? 0.3265 0.3924 0.3085 -0.0040 -0.0020 0.0512 136 VAL B CB 2661 C CG1 . VAL B 137 ? 0.2872 0.3495 0.2671 -0.0044 -0.0034 0.0501 136 VAL B CG1 2662 C CG2 . VAL B 137 ? 0.2526 0.3278 0.2400 -0.0057 -0.0024 0.0528 136 VAL B CG2 2663 N N . ALA B 138 ? 0.3308 0.3934 0.3095 -0.0037 -0.0008 0.0468 137 ALA B N 2664 C CA . ALA B 138 ? 0.3038 0.3578 0.2775 -0.0024 -0.0008 0.0452 137 ALA B CA 2665 C C . ALA B 138 ? 0.2978 0.3507 0.2709 -0.0033 -0.0026 0.0447 137 ALA B C 2666 O O . ALA B 138 ? 0.3008 0.3609 0.2773 -0.0052 -0.0028 0.0438 137 ALA B O 2667 C CB . ALA B 138 ? 0.1679 0.2249 0.1426 -0.0027 0.0006 0.0436 137 ALA B CB 2668 N N . ALA B 139 ? 0.3042 0.3489 0.2733 -0.0020 -0.0038 0.0454 138 ALA B N 2669 C CA . ALA B 139 ? 0.2864 0.3298 0.2550 -0.0026 -0.0057 0.0452 138 ALA B CA 2670 C C . ALA B 139 ? 0.3363 0.3728 0.3009 -0.0017 -0.0065 0.0435 138 ALA B C 2671 O O . ALA B 139 ? 0.2911 0.3194 0.2512 0.0003 -0.0062 0.0429 138 ALA B O 2672 C CB . ALA B 139 ? 0.2365 0.2744 0.2028 -0.0016 -0.0067 0.0467 138 ALA B CB 2673 N N . THR B 140 ? 0.3846 0.4259 0.3516 -0.0033 -0.0077 0.0431 139 THR B N 2674 C CA . THR B 140 ? 0.3104 0.3473 0.2749 -0.0028 -0.0092 0.0422 139 THR B CA 2675 C C . THR B 140 ? 0.2592 0.2917 0.2207 -0.0014 -0.0084 0.0411 139 THR B C 2676 O O . THR B 140 ? 0.2578 0.2796 0.2139 0.0007 -0.0094 0.0403 139 THR B O 2677 C CB . THR B 140 ? 0.4274 0.4536 0.3871 -0.0010 -0.0111 0.0421 139 THR B CB 2678 O OG1 . THR B 140 ? 0.3484 0.3666 0.3040 0.0011 -0.0106 0.0427 139 THR B OG1 2679 C CG2 . THR B 140 ? 0.4110 0.4428 0.3742 -0.0027 -0.0121 0.0431 139 THR B CG2 2680 N N . GLY B 141 ? 0.2571 0.2981 0.2222 -0.0027 -0.0066 0.0409 140 GLY B N 2681 C CA . GLY B 141 ? 0.2266 0.2658 0.1899 -0.0018 -0.0055 0.0398 140 GLY B CA 2682 C C . GLY B 141 ? 0.2903 0.3381 0.2570 -0.0039 -0.0058 0.0389 140 GLY B C 2683 O O . GLY B 141 ? 0.2599 0.3181 0.2318 -0.0067 -0.0061 0.0391 140 GLY B O 2684 N N . LYS B 142 ? 0.2490 0.2924 0.2128 -0.0027 -0.0057 0.0378 141 LYS B N 2685 C CA . LYS B 142 ? 0.2795 0.3307 0.2461 -0.0047 -0.0057 0.0366 141 LYS B CA 2686 C C . LYS B 142 ? 0.3257 0.3782 0.2919 -0.0040 -0.0033 0.0353 141 LYS B C 2687 O O . LYS B 142 ? 0.2884 0.3312 0.2497 -0.0013 -0.0029 0.0350 141 LYS B O 2688 C CB . LYS B 142 ? 0.2549 0.3000 0.2186 -0.0041 -0.0081 0.0363 141 LYS B CB 2689 C CG . LYS B 142 ? 0.2872 0.3400 0.2536 -0.0063 -0.0082 0.0348 141 LYS B CG 2690 C CD . LYS B 142 ? 0.3023 0.3488 0.2662 -0.0056 -0.0111 0.0346 141 LYS B CD 2691 C CE . LYS B 142 ? 0.2876 0.3420 0.2544 -0.0082 -0.0115 0.0329 141 LYS B CE 2692 N NZ . LYS B 142 ? 0.3710 0.4286 0.3375 -0.0081 -0.0092 0.0311 141 LYS B NZ 2693 N N . PRO B 143 ? 0.3108 0.3751 0.2821 -0.0065 -0.0016 0.0342 142 PRO B N 2694 C CA . PRO B 143 ? 0.3073 0.3829 0.2846 -0.0097 -0.0019 0.0344 142 PRO B CA 2695 C C . PRO B 143 ? 0.2496 0.3252 0.2280 -0.0092 -0.0015 0.0360 142 PRO B C 2696 O O . PRO B 143 ? 0.2293 0.2956 0.2036 -0.0065 -0.0012 0.0368 142 PRO B O 2697 C CB . PRO B 143 ? 0.1901 0.2756 0.1716 -0.0119 -0.0002 0.0321 142 PRO B CB 2698 C CG . PRO B 143 ? 0.2465 0.3256 0.2246 -0.0092 0.0019 0.0313 142 PRO B CG 2699 C CD . PRO B 143 ? 0.2198 0.2864 0.1914 -0.0063 0.0008 0.0322 142 PRO B CD 2700 N N . VAL B 144 ? 0.2296 0.3156 0.2136 -0.0118 -0.0017 0.0362 143 VAL B N 2701 C CA . VAL B 144 ? 0.3277 0.4138 0.3128 -0.0113 -0.0015 0.0377 143 VAL B CA 2702 C C . VAL B 144 ? 0.3604 0.4436 0.3442 -0.0095 0.0005 0.0372 143 VAL B C 2703 O O . VAL B 144 ? 0.2650 0.3514 0.2498 -0.0098 0.0017 0.0355 143 VAL B O 2704 C CB . VAL B 144 ? 0.2991 0.3974 0.2906 -0.0144 -0.0023 0.0379 143 VAL B CB 2705 C CG1 . VAL B 144 ? 0.2929 0.4004 0.2883 -0.0162 -0.0016 0.0358 143 VAL B CG1 2706 C CG2 . VAL B 144 ? 0.2104 0.3080 0.2027 -0.0138 -0.0024 0.0397 143 VAL B CG2 2707 N N . ALA B 145 ? 0.3152 0.3916 0.2964 -0.0075 0.0007 0.0386 144 ALA B N 2708 C CA . ALA B 145 ? 0.2524 0.3261 0.2325 -0.0060 0.0025 0.0383 144 ALA B CA 2709 C C . ALA B 145 ? 0.3769 0.4615 0.3626 -0.0080 0.0030 0.0377 144 ALA B C 2710 O O . ALA B 145 ? 0.3033 0.3971 0.2936 -0.0105 0.0017 0.0378 144 ALA B O 2711 C CB . ALA B 145 ? 0.2129 0.2769 0.1891 -0.0038 0.0025 0.0396 144 ALA B CB 2712 N N . GLN B 146 ? 0.3660 0.4490 0.3512 -0.0069 0.0045 0.0371 145 GLN B N 2713 C CA . GLN B 146 ? 0.3405 0.4314 0.3298 -0.0082 0.0047 0.0366 145 GLN B CA 2714 C C . GLN B 146 ? 0.3010 0.3877 0.2893 -0.0067 0.0052 0.0382 145 GLN B C 2715 O O . GLN B 146 ? 0.3197 0.3968 0.3035 -0.0044 0.0062 0.0386 145 GLN B O 2716 C CB . GLN B 146 ? 0.2779 0.3702 0.2676 -0.0083 0.0061 0.0343 145 GLN B CB 2717 C CG . GLN B 146 ? 0.4053 0.5049 0.3985 -0.0098 0.0058 0.0333 145 GLN B CG 2718 C CD . GLN B 146 ? 0.5923 0.6916 0.5852 -0.0098 0.0072 0.0307 145 GLN B CD 2719 O OE1 . GLN B 146 ? 0.5141 0.6136 0.5067 -0.0104 0.0075 0.0290 145 GLN B OE1 2720 N NE2 . GLN B 146 ? 0.5512 0.6501 0.5443 -0.0092 0.0082 0.0305 145 GLN B NE2 2721 N N . ILE B 147 ? 0.3055 0.3992 0.2976 -0.0080 0.0042 0.0391 146 ILE B N 2722 C CA . ILE B 147 ? 0.3354 0.4290 0.3280 -0.0069 0.0045 0.0412 146 ILE B CA 2723 C C . ILE B 147 ? 0.4363 0.5379 0.4324 -0.0078 0.0044 0.0410 146 ILE B C 2724 O O . ILE B 147 ? 0.4182 0.5287 0.4179 -0.0100 0.0029 0.0405 146 ILE B O 2725 C CB . ILE B 147 ? 0.3160 0.4116 0.3101 -0.0075 0.0031 0.0433 146 ILE B CB 2726 C CG1 . ILE B 147 ? 0.2971 0.3831 0.2867 -0.0062 0.0030 0.0437 146 ILE B CG1 2727 C CG2 . ILE B 147 ? 0.2777 0.3756 0.2735 -0.0067 0.0033 0.0453 146 ILE B CG2 2728 C CD1 . ILE B 147 ? 0.2346 0.3224 0.2257 -0.0069 0.0017 0.0455 146 ILE B CD1 2729 N N . ASP B 148 ? 0.4062 0.5042 0.4008 -0.0061 0.0059 0.0414 147 ASP B N 2730 C CA . ASP B 148 ? 0.3998 0.5040 0.3970 -0.0065 0.0058 0.0416 147 ASP B CA 2731 C C . ASP B 148 ? 0.3918 0.4938 0.3888 -0.0048 0.0063 0.0440 147 ASP B C 2732 O O . ASP B 148 ? 0.3747 0.4685 0.3684 -0.0030 0.0072 0.0449 147 ASP B O 2733 C CB . ASP B 148 ? 0.3801 0.4826 0.3760 -0.0060 0.0072 0.0396 147 ASP B CB 2734 C CG . ASP B 148 ? 0.4251 0.5296 0.4212 -0.0076 0.0069 0.0371 147 ASP B CG 2735 O OD1 . ASP B 148 ? 0.4747 0.5874 0.4736 -0.0098 0.0055 0.0363 147 ASP B OD1 2736 O OD2 . ASP B 148 ? 0.4181 0.5158 0.4113 -0.0066 0.0080 0.0359 147 ASP B OD2 2737 N N . TRP B 149 ? 0.4018 0.5107 0.4018 -0.0055 0.0057 0.0448 148 TRP B N 2738 C CA . TRP B 149 ? 0.4075 0.5157 0.4080 -0.0041 0.0061 0.0471 148 TRP B CA 2739 C C . TRP B 149 ? 0.4262 0.5350 0.4267 -0.0033 0.0071 0.0469 148 TRP B C 2740 O O . TRP B 149 ? 0.4173 0.5314 0.4192 -0.0046 0.0066 0.0455 148 TRP B O 2741 C CB . TRP B 149 ? 0.3981 0.5147 0.4026 -0.0057 0.0041 0.0488 148 TRP B CB 2742 C CG . TRP B 149 ? 0.4086 0.5250 0.4135 -0.0064 0.0031 0.0494 148 TRP B CG 2743 C CD1 . TRP B 149 ? 0.3973 0.5182 0.4037 -0.0085 0.0016 0.0483 148 TRP B CD1 2744 C CD2 . TRP B 149 ? 0.3176 0.4292 0.3214 -0.0053 0.0035 0.0512 148 TRP B CD2 2745 N NE1 . TRP B 149 ? 0.4046 0.5239 0.4111 -0.0086 0.0011 0.0494 148 TRP B NE1 2746 C CE2 . TRP B 149 ? 0.3647 0.4781 0.3695 -0.0067 0.0022 0.0511 148 TRP B CE2 2747 C CE3 . TRP B 149 ? 0.3727 0.4785 0.3747 -0.0032 0.0047 0.0528 148 TRP B CE3 2748 C CZ2 . TRP B 149 ? 0.3621 0.4715 0.3658 -0.0061 0.0021 0.0526 148 TRP B CZ2 2749 C CZ3 . TRP B 149 ? 0.4191 0.5208 0.4199 -0.0026 0.0046 0.0541 148 TRP B CZ3 2750 C CH2 . TRP B 149 ? 0.3504 0.4538 0.3519 -0.0040 0.0033 0.0540 148 TRP B CH2 2751 N N . GLU B 150 ? 0.4210 0.5243 0.4200 -0.0011 0.0084 0.0483 149 GLU B N 2752 C CA . GLU B 150 ? 0.5400 0.6436 0.5391 -0.0002 0.0094 0.0485 149 GLU B CA 2753 C C . GLU B 150 ? 0.5477 0.6549 0.5492 0.0002 0.0089 0.0510 149 GLU B C 2754 O O . GLU B 150 ? 0.4911 0.5967 0.4927 0.0007 0.0087 0.0526 149 GLU B O 2755 C CB . GLU B 150 ? 0.4358 0.5295 0.4308 0.0022 0.0115 0.0476 149 GLU B CB 2756 C CG . GLU B 150 ? 0.4926 0.5837 0.4856 0.0017 0.0121 0.0450 149 GLU B CG 2757 C CD . GLU B 150 ? 0.5218 0.6026 0.5104 0.0040 0.0139 0.0443 149 GLU B CD 2758 O OE1 . GLU B 150 ? 0.4580 0.5338 0.4451 0.0059 0.0146 0.0457 149 GLU B OE1 2759 O OE2 . GLU B 150 ? 0.5687 0.6464 0.5554 0.0039 0.0146 0.0422 149 GLU B OE2 2760 N N . GLY B 151 ? 0.4961 0.6082 0.4994 0.0000 0.0088 0.0513 150 GLY B N 2761 C CA . GLY B 151 ? 0.5447 0.6623 0.5509 -0.0001 0.0080 0.0535 150 GLY B CA 2762 C C . GLY B 151 ? 0.6616 0.7895 0.6713 -0.0027 0.0055 0.0537 150 GLY B C 2763 O O . GLY B 151 ? 0.8337 0.9644 0.8448 -0.0037 0.0042 0.0543 150 GLY B O 2764 N N . ASP B 152 ? 0.5920 0.7256 0.6028 -0.0037 0.0048 0.0532 151 ASP B N 2765 C CA . ASP B 152 ? 0.7060 0.8488 0.7189 -0.0063 0.0023 0.0529 151 ASP B CA 2766 C C . ASP B 152 ? 0.6387 0.7875 0.6545 -0.0067 0.0007 0.0555 151 ASP B C 2767 O O . ASP B 152 ? 0.7157 0.8700 0.7328 -0.0073 -0.0002 0.0564 151 ASP B O 2768 C CB . ASP B 152 ? 0.7312 0.8773 0.7434 -0.0074 0.0021 0.0513 151 ASP B CB 2769 C CG . ASP B 152 ? 0.7099 0.8517 0.7197 -0.0076 0.0032 0.0486 151 ASP B CG 2770 O OD1 . ASP B 152 ? 0.7598 0.8982 0.7688 -0.0076 0.0034 0.0478 151 ASP B OD1 2771 O OD2 . ASP B 152 ? 0.6761 0.8179 0.6849 -0.0077 0.0040 0.0472 151 ASP B OD2 2772 N N . LEU B 153 ? 0.5643 0.7120 0.5810 -0.0065 0.0005 0.0566 152 LEU B N 2773 C CA . LEU B 153 ? 0.5898 0.7428 0.6095 -0.0067 -0.0009 0.0591 152 LEU B CA 2774 C C . LEU B 153 ? 0.6545 0.8138 0.6758 -0.0090 -0.0033 0.0590 152 LEU B C 2775 O O . LEU B 153 ? 0.6504 0.8115 0.6724 -0.0097 -0.0039 0.0600 152 LEU B O 2776 C CB . LEU B 153 ? 0.7014 0.8479 0.7208 -0.0046 0.0009 0.0607 152 LEU B CB 2777 C CG . LEU B 153 ? 0.7492 0.8899 0.7670 -0.0023 0.0031 0.0611 152 LEU B CG 2778 C CD1 . LEU B 153 ? 0.7517 0.8831 0.7672 -0.0001 0.0052 0.0618 152 LEU B CD1 2779 C CD2 . LEU B 153 ? 0.7046 0.8511 0.7249 -0.0023 0.0024 0.0630 152 LEU B CD2 2780 N N . GLY B 154 ? 0.7028 0.8610 0.7225 -0.0103 -0.0037 0.0568 153 GLY B N 2781 C CA . GLY B 154 ? 0.6149 0.7736 0.6338 -0.0124 -0.0047 0.0555 153 GLY B CA 2782 C C . GLY B 154 ? 0.6101 0.7676 0.6271 -0.0136 -0.0050 0.0529 153 GLY B C 2783 O O . GLY B 154 ? 0.6717 0.8292 0.6876 -0.0135 -0.0046 0.0516 153 GLY B O 2784 N N . GLU B 155 ? 0.5569 0.7133 0.5735 -0.0148 -0.0055 0.0521 154 GLU B N 2785 C CA . GLU B 155 ? 0.5956 0.7509 0.6104 -0.0161 -0.0059 0.0496 154 GLU B CA 2786 C C . GLU B 155 ? 0.5443 0.6963 0.5596 -0.0157 -0.0057 0.0499 154 GLU B C 2787 O O . GLU B 155 ? 0.4725 0.6236 0.4894 -0.0148 -0.0056 0.0518 154 GLU B O 2788 C CB . GLU B 155 ? 0.6188 0.7764 0.6322 -0.0183 -0.0068 0.0480 154 GLU B CB 2789 C CG . GLU B 155 ? 0.8038 0.9610 0.8150 -0.0198 -0.0070 0.0453 154 GLU B CG 2790 C CD . GLU B 155 ? 1.0183 1.1770 1.0283 -0.0217 -0.0078 0.0442 154 GLU B CD 2791 O OE1 . GLU B 155 ? 1.0613 1.2228 1.0714 -0.0222 -0.0082 0.0450 154 GLU B OE1 2792 O OE2 . GLU B 155 ? 0.8734 1.0306 0.8822 -0.0226 -0.0080 0.0426 154 GLU B OE2 2793 N N . MET B 156 ? 0.5895 0.7398 0.6035 -0.0162 -0.0057 0.0479 155 MET B N 2794 C CA . MET B 156 ? 0.5121 0.6593 0.5264 -0.0159 -0.0055 0.0480 155 MET B CA 2795 C C . MET B 156 ? 0.4818 0.6285 0.4951 -0.0177 -0.0063 0.0463 155 MET B C 2796 O O . MET B 156 ? 0.5550 0.7032 0.5666 -0.0192 -0.0067 0.0443 155 MET B O 2797 C CB . MET B 156 ? 0.4606 0.6057 0.4742 -0.0149 -0.0047 0.0471 155 MET B CB 2798 C CG . MET B 156 ? 0.6533 0.7941 0.6657 -0.0151 -0.0044 0.0460 155 MET B CG 2799 S SD . MET B 156 ? 0.8958 1.0297 0.9047 -0.0142 -0.0024 0.0434 155 MET B SD 2800 C CE . MET B 156 ? 0.6141 0.7429 0.6219 -0.0144 -0.0022 0.0429 155 MET B CE 2801 N N . GLU B 157 ? 0.4004 0.5450 0.4144 -0.0176 -0.0063 0.0471 156 GLU B N 2802 C CA . GLU B 157 ? 0.4896 0.6331 0.5029 -0.0190 -0.0070 0.0457 156 GLU B CA 2803 C C . GLU B 157 ? 0.5151 0.6555 0.5288 -0.0184 -0.0066 0.0461 156 GLU B C 2804 O O . GLU B 157 ? 0.3858 0.5254 0.4010 -0.0172 -0.0062 0.0484 156 GLU B O 2805 C CB . GLU B 157 ? 0.3951 0.5400 0.4092 -0.0197 -0.0076 0.0466 156 GLU B CB 2806 C CG . GLU B 157 ? 0.5716 0.7155 0.5848 -0.0210 -0.0083 0.0452 156 GLU B CG 2807 C CD . GLU B 157 ? 0.6772 0.8213 0.6918 -0.0211 -0.0087 0.0467 156 GLU B CD 2808 O OE1 . GLU B 157 ? 0.7204 0.8632 0.7347 -0.0219 -0.0091 0.0460 156 GLU B OE1 2809 O OE2 . GLU B 157 ? 0.8874 1.0331 0.9035 -0.0204 -0.0085 0.0487 156 GLU B OE2 2810 N N . SER B 158 ? 0.3641 0.5028 0.3764 -0.0194 -0.0068 0.0441 157 SER B N 2811 C CA . SER B 158 ? 0.3877 0.5235 0.4001 -0.0189 -0.0065 0.0444 157 SER B CA 2812 C C . SER B 158 ? 0.4830 0.6171 0.4947 -0.0203 -0.0070 0.0429 157 SER B C 2813 O O . SER B 158 ? 0.4246 0.5596 0.4351 -0.0215 -0.0075 0.0409 157 SER B O 2814 C CB . SER B 158 ? 0.3667 0.5015 0.3782 -0.0182 -0.0059 0.0434 157 SER B CB 2815 O OG . SER B 158 ? 0.4141 0.5492 0.4239 -0.0195 -0.0061 0.0406 157 SER B OG 2816 N N . SER B 159 ? 0.3880 0.5206 0.4005 -0.0202 -0.0069 0.0443 158 SER B N 2817 C CA . SER B 159 ? 0.3792 0.5113 0.3913 -0.0215 -0.0074 0.0435 158 SER B CA 2818 C C . SER B 159 ? 0.3467 0.4772 0.3585 -0.0211 -0.0071 0.0443 158 SER B C 2819 O O . SER B 159 ? 0.4535 0.5779 0.4630 -0.0190 -0.0060 0.0454 158 SER B O 2820 C CB . SER B 159 ? 0.2838 0.4156 0.2969 -0.0220 -0.0078 0.0448 158 SER B CB 2821 O OG . SER B 159 ? 0.5147 0.6479 0.5279 -0.0223 -0.0081 0.0441 158 SER B OG 2822 N N . THR B 160 ? 0.2791 0.4092 0.2900 -0.0223 -0.0074 0.0428 159 THR B N 2823 C CA . THR B 160 ? 0.3229 0.4514 0.3331 -0.0222 -0.0072 0.0433 159 THR B CA 2824 C C . THR B 160 ? 0.3095 0.4372 0.3199 -0.0236 -0.0078 0.0436 159 THR B C 2825 O O . THR B 160 ? 0.3248 0.4532 0.3348 -0.0250 -0.0080 0.0419 159 THR B O 2826 C CB . THR B 160 ? 0.2746 0.4039 0.2836 -0.0223 -0.0069 0.0410 159 THR B CB 2827 O OG1 . THR B 160 ? 0.2841 0.4132 0.2926 -0.0209 -0.0062 0.0407 159 THR B OG1 2828 C CG2 . THR B 160 ? 0.3091 0.4308 0.3142 -0.0212 -0.0061 0.0406 159 THR B CG2 2829 N N . THR B 161 ? 0.2946 0.4121 0.3003 -0.0218 -0.0078 0.0445 160 THR B N 2830 C CA . THR B 161 ? 0.3356 0.4509 0.3405 -0.0229 -0.0087 0.0447 160 THR B CA 2831 C C . THR B 161 ? 0.3211 0.4277 0.3208 -0.0213 -0.0091 0.0437 160 THR B C 2832 O O . THR B 161 ? 0.3518 0.4476 0.3462 -0.0182 -0.0092 0.0438 160 THR B O 2833 C CB . THR B 161 ? 0.2746 0.3841 0.2778 -0.0218 -0.0095 0.0462 160 THR B CB 2834 O OG1 . THR B 161 ? 0.3643 0.4824 0.3725 -0.0234 -0.0092 0.0472 160 THR B OG1 2835 C CG2 . THR B 161 ? 0.3074 0.4141 0.3094 -0.0227 -0.0108 0.0461 160 THR B CG2 2836 N N . SER B 162 ? 0.2512 0.3622 0.2525 -0.0234 -0.0094 0.0425 161 SER B N 2837 C CA . SER B 162 ? 0.3097 0.4130 0.3065 -0.0220 -0.0102 0.0415 161 SER B CA 2838 C C . SER B 162 ? 0.3334 0.4305 0.3280 -0.0217 -0.0122 0.0419 161 SER B C 2839 O O . SER B 162 ? 0.3596 0.4614 0.3572 -0.0238 -0.0125 0.0425 161 SER B O 2840 C CB . SER B 162 ? 0.2762 0.3872 0.2755 -0.0241 -0.0093 0.0396 161 SER B CB 2841 O OG . SER B 162 ? 0.3181 0.4404 0.3229 -0.0279 -0.0087 0.0393 161 SER B OG 2842 N N . PHE B 163 ? 0.3887 0.4748 0.3779 -0.0191 -0.0135 0.0414 162 PHE B N 2843 C CA . PHE B 163 ? 0.3219 0.3995 0.3081 -0.0178 -0.0158 0.0416 162 PHE B CA 2844 C C . PHE B 163 ? 0.2628 0.3379 0.2477 -0.0179 -0.0172 0.0402 162 PHE B C 2845 O O . PHE B 163 ? 0.3138 0.3910 0.2985 -0.0182 -0.0164 0.0391 162 PHE B O 2846 C CB . PHE B 163 ? 0.3195 0.3849 0.3001 -0.0140 -0.0162 0.0422 162 PHE B CB 2847 C CG . PHE B 163 ? 0.3243 0.3914 0.3060 -0.0137 -0.0149 0.0434 162 PHE B CG 2848 C CD1 . PHE B 163 ? 0.3125 0.3826 0.2966 -0.0148 -0.0153 0.0444 162 PHE B CD1 2849 C CD2 . PHE B 163 ? 0.2872 0.3529 0.2675 -0.0122 -0.0132 0.0435 162 PHE B CD2 2850 C CE1 . PHE B 163 ? 0.2991 0.3708 0.2843 -0.0145 -0.0142 0.0455 162 PHE B CE1 2851 C CE2 . PHE B 163 ? 0.3209 0.3882 0.3024 -0.0120 -0.0121 0.0445 162 PHE B CE2 2852 C CZ . PHE B 163 ? 0.3421 0.4125 0.3261 -0.0131 -0.0126 0.0455 162 PHE B CZ 2853 N N . PRO B 164 ? 0.3776 0.4483 0.3616 -0.0178 -0.0194 0.0401 163 PRO B N 2854 C CA . PRO B 164 ? 0.3624 0.4313 0.3458 -0.0181 -0.0210 0.0387 163 PRO B CA 2855 C C . PRO B 164 ? 0.2978 0.3593 0.2768 -0.0156 -0.0212 0.0378 163 PRO B C 2856 O O . PRO B 164 ? 0.3885 0.4528 0.3685 -0.0167 -0.0214 0.0364 163 PRO B O 2857 C CB . PRO B 164 ? 0.3492 0.4121 0.3314 -0.0175 -0.0233 0.0390 163 PRO B CB 2858 C CG . PRO B 164 ? 0.3548 0.4218 0.3393 -0.0185 -0.0225 0.0404 163 PRO B CG 2859 C CD . PRO B 164 ? 0.4776 0.5455 0.4615 -0.0175 -0.0204 0.0412 163 PRO B CD 2860 N N . ASN B 165 ? 0.3044 0.3567 0.2788 -0.0124 -0.0210 0.0384 164 ASN B N 2861 C CA . ASN B 165 ? 0.3274 0.3722 0.2974 -0.0099 -0.0210 0.0376 164 ASN B CA 2862 C C . ASN B 165 ? 0.3693 0.4202 0.3406 -0.0106 -0.0186 0.0372 164 ASN B C 2863 O O . ASN B 165 ? 0.3795 0.4247 0.3473 -0.0085 -0.0181 0.0366 164 ASN B O 2864 C CB . ASN B 165 ? 0.2365 0.2686 0.2008 -0.0060 -0.0214 0.0380 164 ASN B CB 2865 C CG . ASN B 165 ? 0.4255 0.4574 0.3892 -0.0052 -0.0196 0.0391 164 ASN B CG 2866 O OD1 . ASN B 165 ? 0.3656 0.4058 0.3326 -0.0069 -0.0177 0.0395 164 ASN B OD1 2867 N ND2 . ASN B 165 ? 0.3998 0.4222 0.3593 -0.0025 -0.0200 0.0393 164 ASN B ND2 2868 N N . GLU B 166 ? 0.3131 0.3754 0.2893 -0.0134 -0.0169 0.0374 165 GLU B N 2869 C CA . GLU B 166 ? 0.3682 0.4384 0.3467 -0.0146 -0.0144 0.0367 165 GLU B CA 2870 C C . GLU B 166 ? 0.3350 0.4017 0.3113 -0.0124 -0.0125 0.0375 165 GLU B C 2871 O O . GLU B 166 ? 0.3667 0.4377 0.3439 -0.0127 -0.0105 0.0367 165 GLU B O 2872 C CB . GLU B 166 ? 0.3612 0.4315 0.3386 -0.0147 -0.0144 0.0349 165 GLU B CB 2873 C CG . GLU B 166 ? 0.3443 0.4189 0.3243 -0.0171 -0.0161 0.0336 165 GLU B CG 2874 C CD . GLU B 166 ? 0.4534 0.5320 0.4340 -0.0180 -0.0152 0.0314 165 GLU B CD 2875 O OE1 . GLU B 166 ? 0.5560 0.6439 0.5396 -0.0199 -0.0127 0.0303 165 GLU B OE1 2876 O OE2 . GLU B 166 ? 0.5936 0.6657 0.5714 -0.0167 -0.0170 0.0305 165 GLU B OE2 2877 N N . THR B 167 ? 0.2359 0.2945 0.2093 -0.0102 -0.0131 0.0387 166 THR B N 2878 C CA . THR B 167 ? 0.2805 0.3376 0.2531 -0.0089 -0.0113 0.0394 166 THR B CA 2879 C C . THR B 167 ? 0.3607 0.4283 0.3388 -0.0114 -0.0104 0.0403 166 THR B C 2880 O O . THR B 167 ? 0.3351 0.4090 0.3168 -0.0138 -0.0114 0.0406 166 THR B O 2881 C CB . THR B 167 ? 0.2758 0.3195 0.2426 -0.0056 -0.0121 0.0400 166 THR B CB 2882 O OG1 . THR B 167 ? 0.2900 0.3327 0.2574 -0.0059 -0.0136 0.0408 166 THR B OG1 2883 C CG2 . THR B 167 ? 0.3442 0.3775 0.3057 -0.0031 -0.0131 0.0390 166 THR B CG2 2884 N N . ALA B 168 ? 0.3247 0.3942 0.3036 -0.0109 -0.0086 0.0407 167 ALA B N 2885 C CA . ALA B 168 ? 0.3212 0.4009 0.3056 -0.0131 -0.0078 0.0415 167 ALA B CA 2886 C C . ALA B 168 ? 0.3318 0.4065 0.3144 -0.0110 -0.0068 0.0425 167 ALA B C 2887 O O . ALA B 168 ? 0.3789 0.4461 0.3574 -0.0086 -0.0059 0.0421 167 ALA B O 2888 C CB . ALA B 168 ? 0.2161 0.3076 0.2054 -0.0155 -0.0065 0.0403 167 ALA B CB 2889 N N . THR B 169 ? 0.3325 0.4111 0.3179 -0.0120 -0.0071 0.0436 168 THR B N 2890 C CA . THR B 169 ? 0.3091 0.3850 0.2938 -0.0106 -0.0061 0.0445 168 THR B CA 2891 C C . THR B 169 ? 0.3111 0.3992 0.3020 -0.0126 -0.0052 0.0447 168 THR B C 2892 O O . THR B 169 ? 0.3434 0.4414 0.3394 -0.0153 -0.0059 0.0449 168 THR B O 2893 C CB . THR B 169 ? 0.3427 0.4139 0.3260 -0.0100 -0.0073 0.0456 168 THR B CB 2894 O OG1 . THR B 169 ? 0.3251 0.3838 0.3021 -0.0076 -0.0084 0.0451 168 THR B OG1 2895 C CG2 . THR B 169 ? 0.3294 0.4010 0.3135 -0.0092 -0.0063 0.0469 168 THR B CG2 2896 N N . ILE B 170 ? 0.2684 0.3555 0.2587 -0.0114 -0.0038 0.0446 169 ILE B N 2897 C CA . ILE B 170 ? 0.2695 0.3672 0.2653 -0.0130 -0.0033 0.0447 169 ILE B CA 2898 C C . ILE B 170 ? 0.3096 0.4045 0.3049 -0.0117 -0.0029 0.0460 169 ILE B C 2899 O O . ILE B 170 ? 0.2627 0.3491 0.2537 -0.0093 -0.0021 0.0466 169 ILE B O 2900 C CB . ILE B 170 ? 0.1935 0.2947 0.1901 -0.0131 -0.0023 0.0432 169 ILE B CB 2901 C CG1 . ILE B 170 ? 0.2946 0.4052 0.2960 -0.0144 -0.0025 0.0432 169 ILE B CG1 2902 C CG2 . ILE B 170 ? 0.1325 0.2230 0.1236 -0.0102 -0.0008 0.0428 169 ILE B CG2 2903 C CD1 . ILE B 170 ? 0.2433 0.3577 0.2456 -0.0147 -0.0020 0.0415 169 ILE B CD1 2904 N N . VAL B 171 ? 0.2899 0.3940 0.2903 -0.0135 -0.0036 0.0470 170 VAL B N 2905 C CA . VAL B 171 ? 0.3237 0.4296 0.3257 -0.0129 -0.0035 0.0491 170 VAL B CA 2906 C C . VAL B 171 ? 0.3699 0.4854 0.3763 -0.0139 -0.0035 0.0489 170 VAL B C 2907 O O . VAL B 171 ? 0.3793 0.5039 0.3899 -0.0161 -0.0048 0.0482 170 VAL B O 2908 C CB . VAL B 171 ? 0.2969 0.4050 0.3008 -0.0139 -0.0046 0.0505 170 VAL B CB 2909 C CG1 . VAL B 171 ? 0.2607 0.3715 0.2666 -0.0134 -0.0044 0.0526 170 VAL B CG1 2910 C CG2 . VAL B 171 ? 0.2796 0.3773 0.2783 -0.0126 -0.0049 0.0506 170 VAL B CG2 2911 N N . SER B 172 ? 0.2820 0.3951 0.2872 -0.0122 -0.0024 0.0496 171 SER B N 2912 C CA . SER B 172 ? 0.3337 0.4545 0.3422 -0.0128 -0.0026 0.0495 171 SER B CA 2913 C C . SER B 172 ? 0.3790 0.5014 0.3890 -0.0119 -0.0024 0.0518 171 SER B C 2914 O O . SER B 172 ? 0.3959 0.5104 0.4026 -0.0098 -0.0011 0.0527 171 SER B O 2915 C CB . SER B 172 ? 0.3536 0.4707 0.3595 -0.0117 -0.0013 0.0480 171 SER B CB 2916 O OG . SER B 172 ? 0.4741 0.5973 0.4824 -0.0119 -0.0015 0.0482 171 SER B OG 2917 N N . GLN B 173 ? 0.3984 0.5307 0.4131 -0.0136 -0.0040 0.0526 172 GLN B N 2918 C CA . GLN B 173 ? 0.4370 0.5725 0.4539 -0.0130 -0.0041 0.0548 172 GLN B CA 2919 C C . GLN B 173 ? 0.4736 0.6138 0.4916 -0.0129 -0.0043 0.0546 172 GLN B C 2920 O O . GLN B 173 ? 0.4614 0.6054 0.4795 -0.0143 -0.0053 0.0529 172 GLN B O 2921 C CB . GLN B 173 ? 0.4115 0.5536 0.4318 -0.0147 -0.0058 0.0557 172 GLN B CB 2922 C CG . GLN B 173 ? 0.4470 0.5864 0.4673 -0.0149 -0.0058 0.0567 172 GLN B CG 2923 C CD . GLN B 173 ? 0.5733 0.7145 0.5942 -0.0167 -0.0068 0.0559 172 GLN B CD 2924 O OE1 . GLN B 173 ? 0.5734 0.7164 0.5938 -0.0175 -0.0072 0.0545 172 GLN B OE1 2925 N NE2 . GLN B 173 ? 0.7405 0.8804 0.7618 -0.0172 -0.0070 0.0566 172 GLN B NE2 2926 N N . TYR B 174 ? 0.3789 0.5163 0.3962 -0.0111 -0.0031 0.0560 173 TYR B N 2927 C CA . TYR B 174 ? 0.4393 0.5807 0.4576 -0.0109 -0.0032 0.0562 173 TYR B CA 2928 C C . TYR B 174 ? 0.5467 0.6953 0.5685 -0.0115 -0.0045 0.0581 173 TYR B C 2929 O O . TYR B 174 ? 0.4511 0.5983 0.4738 -0.0105 -0.0039 0.0601 173 TYR B O 2930 C CB . TYR B 174 ? 0.4157 0.5489 0.4308 -0.0084 -0.0008 0.0563 173 TYR B CB 2931 C CG . TYR B 174 ? 0.5244 0.6603 0.5396 -0.0083 -0.0006 0.0556 173 TYR B CG 2932 C CD1 . TYR B 174 ? 0.4607 0.5974 0.4748 -0.0091 -0.0008 0.0534 173 TYR B CD1 2933 C CD2 . TYR B 174 ? 0.5626 0.7003 0.5790 -0.0073 -0.0002 0.0573 173 TYR B CD2 2934 C CE1 . TYR B 174 ? 0.5606 0.6994 0.5745 -0.0091 -0.0006 0.0527 173 TYR B CE1 2935 C CE2 . TYR B 174 ? 0.4736 0.6136 0.4900 -0.0072 -0.0001 0.0567 173 TYR B CE2 2936 C CZ . TYR B 174 ? 0.5416 0.6821 0.5566 -0.0081 -0.0003 0.0544 173 TYR B CZ 2937 O OH . TYR B 174 ? 0.5958 0.7383 0.6105 -0.0081 -0.0001 0.0537 173 TYR B OH 2938 N N . LYS B 175 ? 0.5513 0.7020 0.5720 -0.0131 -0.0053 0.0564 174 LYS B N 2939 C CA . LYS B 175 ? 0.5980 0.7512 0.6193 -0.0139 -0.0059 0.0571 174 LYS B CA 2940 C C . LYS B 175 ? 0.6189 0.7746 0.6404 -0.0134 -0.0057 0.0577 174 LYS B C 2941 O O . LYS B 175 ? 0.5849 0.7410 0.6050 -0.0136 -0.0056 0.0563 174 LYS B O 2942 C CB . LYS B 175 ? 0.5825 0.7365 0.6024 -0.0160 -0.0069 0.0551 174 LYS B CB 2943 C CG . LYS B 175 ? 0.6654 0.8174 0.6855 -0.0166 -0.0072 0.0549 174 LYS B CG 2944 C CD . LYS B 175 ? 0.6682 0.8194 0.6864 -0.0182 -0.0078 0.0522 174 LYS B CD 2945 C CE . LYS B 175 ? 0.8028 0.9566 0.8196 -0.0196 -0.0086 0.0510 174 LYS B CE 2946 N NZ . LYS B 175 ? 0.8443 0.9981 0.8613 -0.0204 -0.0093 0.0511 174 LYS B NZ 2947 N N . LEU B 176 ? 0.6386 0.7959 0.6616 -0.0128 -0.0057 0.0597 175 LEU B N 2948 C CA . LEU B 176 ? 0.6761 0.8360 0.6993 -0.0124 -0.0056 0.0603 175 LEU B CA 2949 C C . LEU B 176 ? 0.5296 0.6918 0.5540 -0.0128 -0.0061 0.0618 175 LEU B C 2950 O O . LEU B 176 ? 0.4335 0.5949 0.4592 -0.0125 -0.0061 0.0630 175 LEU B O 2951 C CB . LEU B 176 ? 0.5547 0.7135 0.5789 -0.0102 -0.0044 0.0619 175 LEU B CB 2952 C CG . LEU B 176 ? 0.6100 0.7669 0.6363 -0.0081 -0.0035 0.0644 175 LEU B CG 2953 C CD1 . LEU B 176 ? 0.5965 0.7552 0.6246 -0.0076 -0.0034 0.0665 175 LEU B CD1 2954 C CD2 . LEU B 176 ? 0.6217 0.7724 0.6459 -0.0059 -0.0014 0.0642 175 LEU B CD2 2955 N N . PHE B 177 ? 0.5773 0.7424 0.6013 -0.0133 -0.0064 0.0617 176 PHE B N 2956 C CA . PHE B 177 ? 0.5982 0.7657 0.6235 -0.0133 -0.0067 0.0634 176 PHE B CA 2957 C C . PHE B 177 ? 0.5650 0.7323 0.5921 -0.0112 -0.0057 0.0657 176 PHE B C 2958 O O . PHE B 177 ? 0.5593 0.7271 0.5861 -0.0105 -0.0052 0.0657 176 PHE B O 2959 C CB . PHE B 177 ? 0.6374 0.8081 0.6613 -0.0148 -0.0075 0.0624 176 PHE B CB 2960 C CG . PHE B 177 ? 0.6087 0.7796 0.6305 -0.0168 -0.0084 0.0601 176 PHE B CG 2961 C CD1 . PHE B 177 ? 0.6025 0.7729 0.6224 -0.0175 -0.0084 0.0580 176 PHE B CD1 2962 C CD2 . PHE B 177 ? 0.5566 0.7284 0.5784 -0.0178 -0.0091 0.0601 176 PHE B CD2 2963 C CE1 . PHE B 177 ? 0.6608 0.8314 0.6787 -0.0193 -0.0090 0.0559 176 PHE B CE1 2964 C CE2 . PHE B 177 ? 0.6632 0.8350 0.6829 -0.0195 -0.0098 0.0580 176 PHE B CE2 2965 C CZ . PHE B 177 ? 0.7686 0.9399 0.7864 -0.0202 -0.0098 0.0560 176 PHE B CZ 2966 N N . PRO B 178 ? 0.4471 0.6136 0.4762 -0.0100 -0.0052 0.0678 177 PRO B N 2967 C CA . PRO B 178 ? 0.5352 0.7012 0.5660 -0.0077 -0.0040 0.0701 177 PRO B CA 2968 C C . PRO B 178 ? 0.6374 0.8065 0.6686 -0.0077 -0.0042 0.0709 177 PRO B C 2969 O O . PRO B 178 ? 0.6795 0.8511 0.7106 -0.0090 -0.0051 0.0709 177 PRO B O 2970 C CB . PRO B 178 ? 0.5791 0.7443 0.6118 -0.0069 -0.0037 0.0720 177 PRO B CB 2971 C CG . PRO B 178 ? 0.5224 0.6867 0.5542 -0.0085 -0.0045 0.0706 177 PRO B CG 2972 C CD . PRO B 178 ? 0.4169 0.5829 0.4467 -0.0105 -0.0056 0.0682 177 PRO B CD 2973 N N . THR B 179 ? 0.6845 0.8532 0.7160 -0.0061 -0.0033 0.0716 178 THR B N 2974 C CA . THR B 179 ? 0.6920 0.8633 0.7241 -0.0059 -0.0033 0.0726 178 THR B CA 2975 C C . THR B 179 ? 0.7730 0.9428 0.8068 -0.0031 -0.0018 0.0747 178 THR B C 2976 O O . THR B 179 ? 0.8023 0.9690 0.8367 -0.0014 -0.0008 0.0753 178 THR B O 2977 C CB . THR B 179 ? 0.5791 0.7522 0.6092 -0.0072 -0.0039 0.0708 178 THR B CB 2978 O OG1 . THR B 179 ? 0.7021 0.8730 0.7314 -0.0062 -0.0032 0.0698 178 THR B OG1 2979 C CG2 . THR B 179 ? 0.7018 0.8764 0.7301 -0.0097 -0.0052 0.0686 178 THR B CG2 2980 N N . ARG B 180 ? 0.7672 0.9391 0.8017 -0.0027 -0.0017 0.0759 179 ARG B N 2981 C CA . ARG B 180 ? 0.7673 0.9379 0.8033 0.0000 -0.0002 0.0778 179 ARG B CA 2982 C C . ARG B 180 ? 0.7708 0.9385 0.8054 0.0010 0.0006 0.0766 179 ARG B C 2983 O O . ARG B 180 ? 0.7405 0.8998 0.7729 0.0030 0.0031 0.0763 179 ARG B O 2984 C CB . ARG B 180 ? 0.8810 1.0546 0.9178 -0.0001 -0.0004 0.0791 179 ARG B CB 2985 C CG . ARG B 180 ? 0.9863 1.1587 1.0253 0.0027 0.0011 0.0816 179 ARG B CG 2986 C CD . ARG B 180 ? 1.0285 1.1966 1.0683 0.0045 0.0025 0.0826 179 ARG B CD 2987 N NE . ARG B 180 ? 1.0183 1.1885 1.0592 0.0032 0.0015 0.0832 179 ARG B NE 2988 C CZ . ARG B 180 ? 1.0136 1.1816 1.0556 0.0044 0.0024 0.0845 179 ARG B CZ 2989 N NH1 . ARG B 180 ? 0.9468 1.1060 0.9862 0.0065 0.0049 0.0844 179 ARG B NH1 2990 N NH2 . ARG B 180 ? 0.9337 1.1034 0.9764 0.0031 0.0014 0.0847 179 ARG B NH2 2991 N N . PHE B 181 ? 0.6171 0.7868 0.6499 -0.0007 -0.0004 0.0745 180 PHE B N 2992 C CA . PHE B 181 ? 0.7524 0.9178 0.7828 -0.0001 0.0008 0.0727 180 PHE B CA 2993 C C . PHE B 181 ? 0.8778 1.0350 0.9056 0.0007 0.0024 0.0710 180 PHE B C 2994 O O . PHE B 181 ? 0.8725 1.0224 0.8975 0.0022 0.0044 0.0698 180 PHE B O 2995 C CB . PHE B 181 ? 0.8116 0.9823 0.8412 -0.0023 -0.0010 0.0710 180 PHE B CB 2996 C CG . PHE B 181 ? 0.8826 1.0482 0.9092 -0.0020 0.0003 0.0686 180 PHE B CG 2997 C CD1 . PHE B 181 ? 0.8531 1.0150 0.8785 -0.0005 0.0020 0.0684 180 PHE B CD1 2998 C CD2 . PHE B 181 ? 0.9557 1.1198 0.9805 -0.0032 0.0000 0.0663 180 PHE B CD2 2999 C CE1 . PHE B 181 ? 0.9375 1.0944 0.9600 -0.0002 0.0034 0.0661 180 PHE B CE1 3000 C CE2 . PHE B 181 ? 0.8944 1.0535 0.9164 -0.0029 0.0013 0.0640 180 PHE B CE2 3001 C CZ . PHE B 181 ? 0.9022 1.0576 0.9230 -0.0014 0.0030 0.0638 180 PHE B CZ 3002 N N . ALA B 182 ? 0.8342 0.9924 0.8627 -0.0003 0.0015 0.0710 181 ALA B N 3003 C CA . ALA B 182 ? 0.7520 0.9028 0.7779 0.0002 0.0027 0.0696 181 ALA B CA 3004 C C . ALA B 182 ? 0.7209 0.8643 0.7457 0.0024 0.0047 0.0707 181 ALA B C 3005 O O . ALA B 182 ? 0.8212 0.9568 0.8428 0.0032 0.0060 0.0695 181 ALA B O 3006 C CB . ALA B 182 ? 0.7496 0.9047 0.7766 -0.0018 0.0007 0.0690 181 ALA B CB 3007 N N . ARG B 183 ? 0.7984 0.9437 0.8252 0.0033 0.0049 0.0730 182 ARG B N 3008 C CA . ARG B 183 ? 0.8527 0.9909 0.8781 0.0052 0.0067 0.0740 182 ARG B CA 3009 C C . ARG B 183 ? 0.7753 0.9038 0.7966 0.0073 0.0091 0.0729 182 ARG B C 3010 O O . ARG B 183 ? 0.6736 0.8022 0.6945 0.0077 0.0095 0.0723 182 ARG B O 3011 C CB . ARG B 183 ? 0.7554 0.8980 0.7840 0.0058 0.0066 0.0766 182 ARG B CB 3012 C CG . ARG B 183 ? 0.9121 1.0477 0.9392 0.0075 0.0083 0.0777 182 ARG B CG 3013 C CD . ARG B 183 ? 0.9206 1.0611 0.9511 0.0081 0.0081 0.0802 182 ARG B CD 3014 N NE . ARG B 183 ? 0.9481 1.0817 0.9769 0.0102 0.0101 0.0813 182 ARG B NE 3015 C CZ . ARG B 183 ? 1.0059 1.1408 1.0364 0.0115 0.0108 0.0830 182 ARG B CZ 3016 N NH1 . ARG B 183 ? 1.0251 1.1674 1.0586 0.0109 0.0097 0.0837 182 ARG B NH1 3017 N NH2 . ARG B 183 ? 0.9954 1.1239 1.0242 0.0133 0.0126 0.0838 182 ARG B NH2 3018 N N . GLY B 184 ? 0.8253 0.9452 0.8434 0.0085 0.0104 0.0726 183 GLY B N 3019 C CA . GLY B 184 ? 0.8651 0.9752 0.8789 0.0106 0.0125 0.0715 183 GLY B CA 3020 C C . GLY B 184 ? 0.8229 0.9292 0.8338 0.0104 0.0128 0.0690 183 GLY B C 3021 O O . GLY B 184 ? 0.8287 0.9262 0.8356 0.0120 0.0143 0.0680 183 GLY B O 3022 N N . ARG B 185 ? 0.7670 0.8795 0.7795 0.0083 0.0112 0.0680 184 ARG B N 3023 C CA . ARG B 185 ? 0.8426 0.9517 0.8525 0.0081 0.0116 0.0656 184 ARG B CA 3024 C C . ARG B 185 ? 0.6937 0.7974 0.7007 0.0077 0.0115 0.0644 184 ARG B C 3025 O O . ARG B 185 ? 0.6153 0.7199 0.6230 0.0071 0.0107 0.0653 184 ARG B O 3026 C CB . ARG B 185 ? 0.7980 0.9159 0.8106 0.0061 0.0100 0.0649 184 ARG B CB 3027 C CG . ARG B 185 ? 0.7209 0.8429 0.7354 0.0065 0.0101 0.0658 184 ARG B CG 3028 C CD . ARG B 185 ? 0.7716 0.9022 0.7881 0.0043 0.0083 0.0650 184 ARG B CD 3029 N NE . ARG B 185 ? 1.0063 1.1341 1.0203 0.0037 0.0085 0.0624 184 ARG B NE 3030 C CZ . ARG B 185 ? 1.0382 1.1639 1.0507 0.0042 0.0095 0.0610 184 ARG B CZ 3031 N NH1 . ARG B 185 ? 1.0217 1.1478 1.0348 0.0053 0.0102 0.0621 184 ARG B NH1 3032 N NH2 . ARG B 185 ? 1.0177 1.1410 1.0280 0.0035 0.0098 0.0586 184 ARG B NH2 3033 N N . ARG B 186 ? 0.6935 0.7914 0.6971 0.0082 0.0123 0.0623 185 ARG B N 3034 C CA . ARG B 186 ? 0.6523 0.7433 0.6523 0.0082 0.0124 0.0610 185 ARG B CA 3035 C C . ARG B 186 ? 0.5474 0.6430 0.5484 0.0062 0.0111 0.0594 185 ARG B C 3036 O O . ARG B 186 ? 0.4477 0.5467 0.4495 0.0055 0.0111 0.0582 185 ARG B O 3037 C CB . ARG B 186 ? 0.6078 0.6885 0.6030 0.0103 0.0141 0.0598 185 ARG B CB 3038 C CG . ARG B 186 ? 0.6093 0.6827 0.6003 0.0104 0.0140 0.0582 185 ARG B CG 3039 C CD . ARG B 186 ? 0.5716 0.6351 0.5580 0.0125 0.0154 0.0569 185 ARG B CD 3040 N NE . ARG B 186 ? 0.6438 0.7028 0.6291 0.0144 0.0165 0.0581 185 ARG B NE 3041 C CZ . ARG B 186 ? 0.6888 0.7421 0.6718 0.0153 0.0165 0.0589 185 ARG B CZ 3042 N NH1 . ARG B 186 ? 0.5336 0.5850 0.5150 0.0144 0.0154 0.0588 185 ARG B NH1 3043 N NH2 . ARG B 186 ? 0.8270 0.8768 0.8093 0.0171 0.0176 0.0599 185 ARG B NH2 3044 N N . ILE B 187 ? 0.5347 0.6304 0.5355 0.0051 0.0101 0.0593 186 ILE B N 3045 C CA . ILE B 187 ? 0.4734 0.5720 0.4745 0.0033 0.0090 0.0577 186 ILE B CA 3046 C C . ILE B 187 ? 0.5139 0.6029 0.5101 0.0042 0.0098 0.0562 186 ILE B C 3047 O O . ILE B 187 ? 0.3909 0.4732 0.3844 0.0052 0.0100 0.0569 186 ILE B O 3048 C CB . ILE B 187 ? 0.4644 0.5711 0.4693 0.0012 0.0071 0.0585 186 ILE B CB 3049 C CG1 . ILE B 187 ? 0.5030 0.6058 0.5069 0.0018 0.0071 0.0600 186 ILE B CG1 3050 C CG2 . ILE B 187 ? 0.5942 0.7115 0.6038 -0.0001 0.0059 0.0595 186 ILE B CG2 3051 C CD1 . ILE B 187 ? 0.4620 0.5716 0.4691 -0.0003 0.0053 0.0606 186 ILE B CD1 3052 N N . THR B 188 ? 0.4963 0.5845 0.4913 0.0037 0.0099 0.0541 187 THR B N 3053 C CA . THR B 188 ? 0.4694 0.5488 0.4598 0.0045 0.0105 0.0526 187 THR B CA 3054 C C . THR B 188 ? 0.4480 0.5307 0.4391 0.0026 0.0093 0.0512 187 THR B C 3055 O O . THR B 188 ? 0.3711 0.4616 0.3654 0.0009 0.0087 0.0504 187 THR B O 3056 C CB . THR B 188 ? 0.4791 0.5539 0.4671 0.0059 0.0120 0.0511 187 THR B CB 3057 O OG1 . THR B 188 ? 0.5535 0.6247 0.5406 0.0078 0.0131 0.0524 187 THR B OG1 3058 C CG2 . THR B 188 ? 0.4451 0.5110 0.4283 0.0066 0.0124 0.0494 187 THR B CG2 3059 N N . CYS B 189 ? 0.4103 0.4867 0.3983 0.0029 0.0089 0.0510 188 CYS B N 3060 C CA . CYS B 189 ? 0.3964 0.4735 0.3840 0.0015 0.0080 0.0496 188 CYS B CA 3061 C C . CYS B 189 ? 0.4706 0.5398 0.4538 0.0026 0.0090 0.0477 188 CYS B C 3062 O O . CYS B 189 ? 0.4241 0.4837 0.4028 0.0045 0.0095 0.0477 188 CYS B O 3063 C CB . CYS B 189 ? 0.4427 0.5174 0.4293 0.0011 0.0069 0.0506 188 CYS B CB 3064 S SG . CYS B 189 ? 0.6275 0.7006 0.6125 -0.0001 0.0060 0.0487 188 CYS B SG 3065 N N . VAL B 190 ? 0.3784 0.4515 0.3629 0.0013 0.0089 0.0459 189 VAL B N 3066 C CA . VAL B 190 ? 0.4101 0.4770 0.3911 0.0022 0.0099 0.0439 189 VAL B CA 3067 C C . VAL B 190 ? 0.4359 0.5030 0.4163 0.0008 0.0090 0.0425 189 VAL B C 3068 O O . VAL B 190 ? 0.3953 0.4709 0.3796 -0.0013 0.0082 0.0419 189 VAL B O 3069 C CB . VAL B 190 ? 0.3994 0.4704 0.3822 0.0020 0.0110 0.0427 189 VAL B CB 3070 C CG1 . VAL B 190 ? 0.3433 0.4086 0.3230 0.0027 0.0122 0.0405 189 VAL B CG1 3071 C CG2 . VAL B 190 ? 0.4054 0.4755 0.3885 0.0035 0.0119 0.0442 189 VAL B CG2 3072 N N . VAL B 191 ? 0.3650 0.4227 0.3405 0.0020 0.0088 0.0421 190 VAL B N 3073 C CA . VAL B 191 ? 0.3145 0.3711 0.2889 0.0011 0.0078 0.0411 190 VAL B CA 3074 C C . VAL B 191 ? 0.3287 0.3799 0.2999 0.0018 0.0087 0.0390 190 VAL B C 3075 O O . VAL B 191 ? 0.2687 0.3109 0.2355 0.0037 0.0091 0.0389 190 VAL B O 3076 C CB . VAL B 191 ? 0.3679 0.4181 0.3392 0.0018 0.0063 0.0423 190 VAL B CB 3077 C CG1 . VAL B 191 ? 0.2939 0.3427 0.2639 0.0009 0.0051 0.0413 190 VAL B CG1 3078 C CG2 . VAL B 191 ? 0.2662 0.3218 0.2408 0.0010 0.0056 0.0444 190 VAL B CG2 3079 N N . LYS B 192 ? 0.3393 0.3963 0.3130 0.0002 0.0089 0.0373 191 LYS B N 3080 C CA . LYS B 192 ? 0.3814 0.4366 0.3535 0.0007 0.0099 0.0356 191 LYS B CA 3081 C C . LYS B 192 ? 0.3251 0.3806 0.2965 0.0002 0.0086 0.0355 191 LYS B C 3082 O O . LYS B 192 ? 0.2977 0.3606 0.2726 -0.0018 0.0073 0.0359 191 LYS B O 3083 C CB . LYS B 192 ? 0.2456 0.3091 0.2219 -0.0006 0.0111 0.0339 191 LYS B CB 3084 C CG . LYS B 192 ? 0.3837 0.4464 0.3590 -0.0004 0.0122 0.0318 191 LYS B CG 3085 C CD . LYS B 192 ? 0.4390 0.5076 0.4178 -0.0016 0.0134 0.0296 191 LYS B CD 3086 C CE . LYS B 192 ? 0.5161 0.5948 0.5000 -0.0042 0.0121 0.0295 191 LYS B CE 3087 N NZ . LYS B 192 ? 0.6282 0.7113 0.6147 -0.0053 0.0130 0.0274 191 LYS B NZ 3088 N N . HIS B 193 ? 0.3406 0.3880 0.3075 0.0018 0.0087 0.0349 192 HIS B N 3089 C CA . HIS B 193 ? 0.2490 0.2960 0.2148 0.0014 0.0073 0.0347 192 HIS B CA 3090 C C . HIS B 193 ? 0.2855 0.3262 0.2476 0.0031 0.0081 0.0334 192 HIS B C 3091 O O . HIS B 193 ? 0.2651 0.2970 0.2233 0.0050 0.0086 0.0334 192 HIS B O 3092 C CB . HIS B 193 ? 0.2771 0.3176 0.2400 0.0019 0.0051 0.0363 192 HIS B CB 3093 C CG . HIS B 193 ? 0.3433 0.3845 0.3059 0.0012 0.0033 0.0363 192 HIS B CG 3094 N ND1 . HIS B 193 ? 0.2629 0.2951 0.2207 0.0028 0.0024 0.0358 192 HIS B ND1 3095 C CD2 . HIS B 193 ? 0.2954 0.3448 0.2619 -0.0010 0.0021 0.0366 192 HIS B CD2 3096 C CE1 . HIS B 193 ? 0.2553 0.2901 0.2139 0.0017 0.0006 0.0359 192 HIS B CE1 3097 N NE2 . HIS B 193 ? 0.2453 0.2906 0.2092 -0.0007 0.0005 0.0364 192 HIS B NE2 3098 N N . PRO B 194 ? 0.2949 0.3398 0.2581 0.0022 0.0080 0.0322 193 PRO B N 3099 C CA . PRO B 194 ? 0.2806 0.3196 0.2403 0.0039 0.0088 0.0308 193 PRO B CA 3100 C C . PRO B 194 ? 0.2724 0.2986 0.2262 0.0064 0.0072 0.0318 193 PRO B C 3101 O O . PRO B 194 ? 0.4343 0.4545 0.3853 0.0083 0.0080 0.0309 193 PRO B O 3102 C CB . PRO B 194 ? 0.2435 0.2902 0.2059 0.0020 0.0087 0.0293 193 PRO B CB 3103 C CG . PRO B 194 ? 0.2696 0.3248 0.2363 -0.0007 0.0072 0.0303 193 PRO B CG 3104 C CD . PRO B 194 ? 0.2107 0.2671 0.1791 -0.0008 0.0075 0.0315 193 PRO B CD 3105 N N . ALA B 195 ? 0.3236 0.3452 0.2756 0.0063 0.0047 0.0334 194 ALA B N 3106 C CA . ALA B 195 ? 0.2890 0.2983 0.2362 0.0079 0.0027 0.0338 194 ALA B CA 3107 C C . ALA B 195 ? 0.3860 0.3893 0.3318 0.0087 0.0031 0.0341 194 ALA B C 3108 O O . ALA B 195 ? 0.4361 0.4309 0.3797 0.0095 0.0013 0.0343 194 ALA B O 3109 C CB . ALA B 195 ? 0.2763 0.2825 0.2223 0.0072 -0.0002 0.0348 194 ALA B CB 3110 N N . LEU B 196 ? 0.3664 0.3748 0.3146 0.0084 0.0051 0.0341 195 LEU B N 3111 C CA . LEU B 196 ? 0.3418 0.3456 0.2892 0.0089 0.0054 0.0345 195 LEU B CA 3112 C C . LEU B 196 ? 0.3592 0.3624 0.3069 0.0104 0.0075 0.0333 195 LEU B C 3113 O O . LEU B 196 ? 0.3776 0.3871 0.3273 0.0104 0.0096 0.0323 195 LEU B O 3114 C CB . LEU B 196 ? 0.3115 0.3210 0.2614 0.0077 0.0062 0.0353 195 LEU B CB 3115 C CG . LEU B 196 ? 0.3875 0.3976 0.3376 0.0066 0.0043 0.0365 195 LEU B CG 3116 C CD1 . LEU B 196 ? 0.3517 0.3701 0.3059 0.0058 0.0054 0.0375 195 LEU B CD1 3117 C CD2 . LEU B 196 ? 0.3590 0.3603 0.3057 0.0076 0.0023 0.0375 195 LEU B CD2 3118 N N . GLU B 197 ? 0.4393 0.4354 0.3858 0.0118 0.0069 0.0333 196 GLU B N 3119 C CA . GLU B 197 ? 0.4202 0.4155 0.3673 0.0138 0.0091 0.0322 196 GLU B CA 3120 C C . GLU B 197 ? 0.4979 0.4979 0.4471 0.0131 0.0109 0.0324 196 GLU B C 3121 O O . GLU B 197 ? 0.4650 0.4673 0.4154 0.0141 0.0130 0.0312 196 GLU B O 3122 C CB . GLU B 197 ? 0.4632 0.4503 0.4092 0.0164 0.0084 0.0321 196 GLU B CB 3123 C CG . GLU B 197 ? 0.6444 0.6269 0.5891 0.0168 0.0065 0.0316 196 GLU B CG 3124 C CD . GLU B 197 ? 0.7230 0.6983 0.6667 0.0203 0.0075 0.0299 196 GLU B CD 3125 O OE1 . GLU B 197 ? 0.7536 0.7232 0.6960 0.0219 0.0068 0.0301 196 GLU B OE1 3126 O OE2 . GLU B 197 ? 0.6584 0.6335 0.6021 0.0218 0.0094 0.0282 196 GLU B OE2 3127 N N A LYS B 198 ? 0.4397 0.4418 0.3895 0.0124 0.0104 0.0341 197 LYS B N 3128 N N B LYS B 198 ? 0.4598 0.4619 0.4097 0.0124 0.0104 0.0341 197 LYS B N 3129 C CA A LYS B 198 ? 0.4552 0.4635 0.4077 0.0120 0.0121 0.0345 197 LYS B CA 3130 C CA B LYS B 198 ? 0.4547 0.4626 0.4072 0.0121 0.0120 0.0347 197 LYS B CA 3131 C C A LYS B 198 ? 0.4734 0.4865 0.4274 0.0103 0.0112 0.0360 197 LYS B C 3132 C C B LYS B 198 ? 0.4695 0.4826 0.4235 0.0103 0.0111 0.0360 197 LYS B C 3133 O O A LYS B 198 ? 0.4253 0.4353 0.3777 0.0100 0.0093 0.0369 197 LYS B O 3134 O O B LYS B 198 ? 0.4120 0.4223 0.3644 0.0099 0.0093 0.0368 197 LYS B O 3135 C CB A LYS B 198 ? 0.4316 0.4369 0.3844 0.0143 0.0131 0.0353 197 LYS B CB 3136 C CB B LYS B 198 ? 0.4301 0.4342 0.3824 0.0145 0.0127 0.0357 197 LYS B CB 3137 C CG A LYS B 198 ? 0.4074 0.4082 0.3589 0.0154 0.0119 0.0370 197 LYS B CG 3138 C CG B LYS B 198 ? 0.4331 0.4390 0.3870 0.0157 0.0149 0.0348 197 LYS B CG 3139 C CD A LYS B 198 ? 0.4053 0.4043 0.3574 0.0176 0.0135 0.0375 197 LYS B CD 3140 C CD B LYS B 198 ? 0.4467 0.4547 0.4023 0.0164 0.0157 0.0363 197 LYS B CD 3141 C CE A LYS B 198 ? 0.4347 0.4306 0.3860 0.0183 0.0127 0.0392 197 LYS B CE 3142 C CE B LYS B 198 ? 0.4221 0.4302 0.3789 0.0182 0.0177 0.0355 197 LYS B CE 3143 N NZ A LYS B 198 ? 0.4912 0.4796 0.4399 0.0195 0.0114 0.0389 197 LYS B NZ 3144 N NZ B LYS B 198 ? 0.4020 0.4145 0.3602 0.0171 0.0188 0.0337 197 LYS B NZ 3145 N N . ASP B 199 ? 0.3802 0.4013 0.3378 0.0093 0.0124 0.0362 198 ASP B N 3146 C CA . ASP B 199 ? 0.3991 0.4265 0.3595 0.0079 0.0117 0.0376 198 ASP B CA 3147 C C . ASP B 199 ? 0.4354 0.4586 0.3944 0.0090 0.0108 0.0396 198 ASP B C 3148 O O . ASP B 199 ? 0.5063 0.5252 0.4641 0.0107 0.0114 0.0401 198 ASP B O 3149 C CB . ASP B 199 ? 0.3609 0.3981 0.3262 0.0068 0.0130 0.0375 198 ASP B CB 3150 C CG . ASP B 199 ? 0.4571 0.4993 0.4244 0.0055 0.0139 0.0353 198 ASP B CG 3151 O OD1 . ASP B 199 ? 0.5353 0.5744 0.5006 0.0052 0.0137 0.0338 198 ASP B OD1 3152 O OD2 . ASP B 199 ? 0.5358 0.5854 0.5070 0.0046 0.0148 0.0349 198 ASP B OD2 3153 N N . ILE B 200 ? 0.3275 0.3521 0.2868 0.0080 0.0094 0.0406 199 ILE B N 3154 C CA . ILE B 200 ? 0.3547 0.3771 0.3136 0.0086 0.0086 0.0425 199 ILE B CA 3155 C C . ILE B 200 ? 0.4120 0.4429 0.3754 0.0081 0.0096 0.0438 199 ILE B C 3156 O O . ILE B 200 ? 0.4206 0.4605 0.3882 0.0064 0.0097 0.0437 199 ILE B O 3157 C CB . ILE B 200 ? 0.3068 0.3276 0.2645 0.0078 0.0067 0.0431 199 ILE B CB 3158 C CG1 . ILE B 200 ? 0.3369 0.3486 0.2900 0.0085 0.0054 0.0420 199 ILE B CG1 3159 C CG2 . ILE B 200 ? 0.3147 0.3347 0.2726 0.0082 0.0062 0.0450 199 ILE B CG2 3160 C CD1 . ILE B 200 ? 0.2846 0.2940 0.2361 0.0077 0.0032 0.0423 199 ILE B CD1 3161 N N . ARG B 201 ? 0.3992 0.4277 0.3623 0.0094 0.0102 0.0450 200 ARG B N 3162 C CA . ARG B 201 ? 0.3506 0.3866 0.3179 0.0091 0.0111 0.0463 200 ARG B CA 3163 C C . ARG B 201 ? 0.4060 0.4399 0.3729 0.0098 0.0107 0.0482 200 ARG B C 3164 O O . ARG B 201 ? 0.4207 0.4467 0.3843 0.0115 0.0109 0.0484 200 ARG B O 3165 C CB . ARG B 201 ? 0.3469 0.3833 0.3149 0.0102 0.0128 0.0457 200 ARG B CB 3166 C CG . ARG B 201 ? 0.3959 0.4357 0.3649 0.0093 0.0134 0.0437 200 ARG B CG 3167 C CD . ARG B 201 ? 0.4104 0.4493 0.3795 0.0106 0.0150 0.0430 200 ARG B CD 3168 N NE . ARG B 201 ? 0.4688 0.5140 0.4416 0.0105 0.0154 0.0444 200 ARG B NE 3169 C CZ . ARG B 201 ? 0.4139 0.4676 0.3906 0.0091 0.0157 0.0440 200 ARG B CZ 3170 N NH1 . ARG B 201 ? 0.3352 0.3919 0.3125 0.0078 0.0157 0.0421 200 ARG B NH1 3171 N NH2 . ARG B 201 ? 0.5006 0.5597 0.4803 0.0090 0.0157 0.0455 200 ARG B NH2 3172 N N . TYR B 202 ? 0.4210 0.4621 0.3916 0.0085 0.0101 0.0496 201 TYR B N 3173 C CA . TYR B 202 ? 0.4053 0.4460 0.3764 0.0090 0.0098 0.0515 201 TYR B CA 3174 C C . TYR B 202 ? 0.4122 0.4627 0.3886 0.0082 0.0103 0.0528 201 TYR B C 3175 O O . TYR B 202 ? 0.4060 0.4651 0.3864 0.0065 0.0100 0.0526 201 TYR B O 3176 C CB . TYR B 202 ? 0.4236 0.4631 0.3938 0.0081 0.0083 0.0520 201 TYR B CB 3177 C CG . TYR B 202 ? 0.4799 0.5091 0.4446 0.0090 0.0074 0.0510 201 TYR B CG 3178 C CD1 . TYR B 202 ? 0.4057 0.4261 0.3664 0.0107 0.0077 0.0511 201 TYR B CD1 3179 C CD2 . TYR B 202 ? 0.4203 0.4488 0.3839 0.0080 0.0063 0.0499 201 TYR B CD2 3180 C CE1 . TYR B 202 ? 0.4750 0.4864 0.4311 0.0113 0.0065 0.0502 201 TYR B CE1 3181 C CE2 . TYR B 202 ? 0.3700 0.3892 0.3286 0.0087 0.0051 0.0490 201 TYR B CE2 3182 C CZ . TYR B 202 ? 0.4968 0.5076 0.4517 0.0103 0.0051 0.0491 201 TYR B CZ 3183 O OH . TYR B 202 ? 0.5536 0.5559 0.5042 0.0107 0.0036 0.0483 201 TYR B OH 3184 N N . SER B 203 ? 0.4874 0.5365 0.4640 0.0094 0.0110 0.0543 202 SER B N 3185 C CA . SER B 203 ? 0.4231 0.4807 0.4045 0.0090 0.0114 0.0557 202 SER B CA 3186 C C . SER B 203 ? 0.5020 0.5582 0.4836 0.0098 0.0116 0.0576 202 SER B C 3187 O O . SER B 203 ? 0.4744 0.5223 0.4520 0.0110 0.0116 0.0578 202 SER B O 3188 C CB . SER B 203 ? 0.5534 0.6114 0.5353 0.0099 0.0128 0.0550 202 SER B CB 3189 O OG . SER B 203 ? 0.5723 0.6212 0.5502 0.0121 0.0138 0.0548 202 SER B OG 3190 N N . PHE B 204 ? 0.6042 0.6687 0.5905 0.0092 0.0116 0.0591 203 PHE B N 3191 C CA . PHE B 204 ? 0.5411 0.6055 0.5283 0.0100 0.0118 0.0611 203 PHE B CA 3192 C C . PHE B 204 ? 0.5922 0.6663 0.5847 0.0094 0.0119 0.0625 203 PHE B C 3193 O O . PHE B 204 ? 0.5448 0.6264 0.5405 0.0080 0.0113 0.0619 203 PHE B O 3194 C CB . PHE B 204 ? 0.5149 0.5787 0.5017 0.0092 0.0107 0.0620 203 PHE B CB 3195 C CG . PHE B 204 ? 0.5261 0.5997 0.5176 0.0069 0.0093 0.0624 203 PHE B CG 3196 C CD1 . PHE B 204 ? 0.4912 0.5653 0.4820 0.0056 0.0083 0.0610 203 PHE B CD1 3197 C CD2 . PHE B 204 ? 0.5648 0.6473 0.5613 0.0061 0.0089 0.0642 203 PHE B CD2 3198 C CE1 . PHE B 204 ? 0.4952 0.5784 0.4904 0.0035 0.0069 0.0614 203 PHE B CE1 3199 C CE2 . PHE B 204 ? 0.5492 0.6408 0.5501 0.0040 0.0074 0.0645 203 PHE B CE2 3200 C CZ . PHE B 204 ? 0.6256 0.7176 0.6259 0.0026 0.0065 0.0631 203 PHE B CZ 3201 N N . ILE B 205 ? 0.6556 0.7294 0.6489 0.0105 0.0125 0.0642 204 ILE B N 3202 C CA . ILE B 205 ? 0.7253 0.8071 0.7232 0.0103 0.0127 0.0656 204 ILE B CA 3203 C C . ILE B 205 ? 0.7322 0.8228 0.7347 0.0086 0.0112 0.0672 204 ILE B C 3204 O O . ILE B 205 ? 0.5930 0.6815 0.5947 0.0086 0.0109 0.0681 204 ILE B O 3205 C CB . ILE B 205 ? 0.7503 0.8272 0.7469 0.0125 0.0142 0.0666 204 ILE B CB 3206 C CG1 . ILE B 205 ? 0.6938 0.7617 0.6857 0.0141 0.0155 0.0649 204 ILE B CG1 3207 C CG2 . ILE B 205 ? 0.7239 0.8090 0.7251 0.0124 0.0143 0.0681 204 ILE B CG2 3208 C CD1 . ILE B 205 ? 0.7084 0.7657 0.6950 0.0153 0.0158 0.0642 204 ILE B CD1 3209 N N . LEU B 206 ? 0.8104 0.9109 0.8175 0.0072 0.0103 0.0676 205 LEU B N 3210 C CA . LEU B 206 ? 0.8123 0.9221 0.8240 0.0055 0.0086 0.0689 205 LEU B CA 3211 C C . LEU B 206 ? 0.8649 0.9760 0.8784 0.0064 0.0090 0.0713 205 LEU B C 3212 O O . LEU B 206 ? 0.8214 0.9320 0.8353 0.0077 0.0100 0.0721 205 LEU B O 3213 C CB . LEU B 206 ? 0.8175 0.9371 0.8330 0.0038 0.0072 0.0686 205 LEU B CB 3214 C CG . LEU B 206 ? 0.7877 0.9089 0.8026 0.0022 0.0063 0.0664 205 LEU B CG 3215 C CD1 . LEU B 206 ? 0.6752 0.8064 0.6937 0.0005 0.0046 0.0663 205 LEU B CD1 3216 C CD2 . LEU B 206 ? 0.7237 0.8447 0.7384 0.0010 0.0053 0.0661 205 LEU B CD2 3217 N N . ASP B 207 ? 0.9105 1.0234 0.9253 0.0057 0.0082 0.0724 206 ASP B N 3218 C CA . ASP B 207 ? 0.8291 0.9445 0.8464 0.0063 0.0084 0.0747 206 ASP B CA 3219 C C . ASP B 207 ? 0.8244 0.9517 0.8474 0.0044 0.0064 0.0759 206 ASP B C 3220 O O . ASP B 207 ? 0.7784 0.9093 0.8028 0.0028 0.0051 0.0757 206 ASP B O 3221 C CB . ASP B 207 ? 0.7932 0.9017 0.8076 0.0070 0.0089 0.0751 206 ASP B CB 3222 C CG . ASP B 207 ? 1.0209 1.1292 1.0364 0.0082 0.0097 0.0773 206 ASP B CG 3223 O OD1 . ASP B 207 ? 0.9557 1.0715 0.9755 0.0081 0.0094 0.0787 206 ASP B OD1 3224 O OD2 . ASP B 207 ? 1.0798 1.1805 1.0919 0.0094 0.0106 0.0775 206 ASP B OD2 3225 N N . ILE B 208 ? 0.8453 0.9788 0.8714 0.0045 0.0061 0.0770 207 ILE B N 3226 C CA . ILE B 208 ? 0.9250 1.0697 0.9562 0.0028 0.0041 0.0783 207 ILE B CA 3227 C C . ILE B 208 ? 0.9832 1.1302 1.0169 0.0038 0.0044 0.0808 207 ILE B C 3228 O O . ILE B 208 ? 1.0520 1.1965 1.0852 0.0054 0.0057 0.0815 207 ILE B O 3229 C CB . ILE B 208 ? 0.8311 0.9818 0.8637 0.0019 0.0029 0.0775 207 ILE B CB 3230 C CG1 . ILE B 208 ? 0.8054 0.9520 0.8349 0.0014 0.0031 0.0749 207 ILE B CG1 3231 C CG2 . ILE B 208 ? 0.8000 0.9619 0.8370 -0.0001 0.0003 0.0785 207 ILE B CG2 3232 C CD1 . ILE B 208 ? 0.8101 0.9631 0.8408 0.0000 0.0016 0.0739 207 ILE B CD1 3233 N N . GLN B 209 ? 0.9510 1.1027 0.9874 0.0028 0.0032 0.0820 208 GLN B N 3234 C CA . GLN B 209 ? 1.0632 1.2170 1.1020 0.0035 0.0035 0.0843 208 GLN B CA 3235 C C . GLN B 209 ? 1.0862 1.2502 1.1299 0.0029 0.0020 0.0863 208 GLN B C 3236 O O . GLN B 209 ? 1.0444 1.2120 1.0881 0.0018 0.0008 0.0853 208 GLN B O 3237 C CB . GLN B 209 ? 1.0169 1.1710 1.0562 0.0025 0.0028 0.0846 208 GLN B CB 3238 C CG . GLN B 209 ? 1.0587 1.2228 1.1020 0.0002 0.0002 0.0847 208 GLN B CG 3239 C CD . GLN B 209 ? 1.1125 1.2774 1.1540 -0.0012 -0.0007 0.0823 208 GLN B CD 3240 O OE1 . GLN B 209 ? 1.1074 1.2705 1.1475 -0.0018 -0.0009 0.0807 208 GLN B OE1 3241 N NE2 . GLN B 209 ? 1.1119 1.2792 1.1531 -0.0018 -0.0012 0.0820 208 GLN B NE2 3242 N N . HIS B 210 ? 1.1265 1.2923 1.1724 0.0035 0.0021 0.0884 209 HIS B N 3243 C CA . HIS B 210 ? 1.1626 1.3329 1.2104 0.0032 0.0016 0.0897 209 HIS B CA 3244 C C . HIS B 210 ? 1.1278 1.3004 1.1749 0.0007 -0.0001 0.0886 209 HIS B C 3245 O O . HIS B 210 ? 1.1004 1.2722 1.1465 -0.0006 -0.0008 0.0872 209 HIS B O 3246 C CB . HIS B 210 ? 1.1916 1.3611 1.2415 0.0055 0.0030 0.0924 209 HIS B CB 3247 C CG . HIS B 210 ? 1.2650 1.4230 1.3100 0.0074 0.0057 0.0913 209 HIS B CG 3248 N ND1 . HIS B 210 ? 1.2137 1.3637 1.2545 0.0074 0.0065 0.0895 209 HIS B ND1 3249 C CD2 . HIS B 210 ? 1.3012 1.4544 1.3446 0.0093 0.0075 0.0917 209 HIS B CD2 3250 C CE1 . HIS B 210 ? 1.1763 1.3170 1.2129 0.0092 0.0086 0.0888 209 HIS B CE1 3251 N NE2 . HIS B 210 ? 1.2965 1.4389 1.3347 0.0104 0.0093 0.0901 209 HIS B NE2 3252 N N . HIS B 211 ? 1.2807 1.4566 1.3281 -0.0003 -0.0010 0.0888 210 HIS B N 3253 C CA . HIS B 211 ? 1.2471 1.4255 1.2940 -0.0025 -0.0025 0.0879 210 HIS B CA 3254 C C . HIS B 211 ? 1.1954 1.3734 1.2399 -0.0045 -0.0036 0.0851 210 HIS B C 3255 O O . HIS B 211 ? 1.2139 1.3936 1.2576 -0.0063 -0.0048 0.0840 210 HIS B O 3256 C CB . HIS B 211 ? 1.2327 1.4111 1.2810 -0.0024 -0.0024 0.0891 210 HIS B CB 3257 C CG . HIS B 211 ? 1.1687 1.3450 1.2161 -0.0032 -0.0027 0.0879 210 HIS B CG 3258 N ND1 . HIS B 211 ? 1.2085 1.3852 1.2543 -0.0053 -0.0040 0.0857 210 HIS B ND1 3259 C CD2 . HIS B 211 ? 1.0970 1.2709 1.1452 -0.0021 -0.0018 0.0888 210 HIS B CD2 3260 C CE1 . HIS B 211 ? 1.1239 1.2984 1.1693 -0.0055 -0.0039 0.0852 210 HIS B CE1 3261 N NE2 . HIS B 211 ? 1.1337 1.3065 1.1806 -0.0036 -0.0026 0.0871 210 HIS B NE2 3262 C C1 . NAG C . ? 0.4131 0.4371 0.4764 -0.0242 0.0336 -0.0579 301 NAG A C1 3263 C C2 . NAG C . ? 0.4038 0.4244 0.4676 -0.0229 0.0328 -0.0558 301 NAG A C2 3264 C C3 . NAG C . ? 0.4789 0.4982 0.5441 -0.0231 0.0338 -0.0561 301 NAG A C3 3265 C C4 . NAG C . ? 0.5281 0.5483 0.5925 -0.0247 0.0350 -0.0579 301 NAG A C4 3266 C C5 . NAG C . ? 0.4953 0.5187 0.5590 -0.0261 0.0358 -0.0600 301 NAG A C5 3267 C C6 . NAG C . ? 0.4845 0.5088 0.5468 -0.0276 0.0365 -0.0614 301 NAG A C6 3268 C C7 . NAG C . ? 0.4544 0.4737 0.5184 -0.0204 0.0304 -0.0527 301 NAG A C7 3269 C C8 . NAG C . ? 0.3372 0.3559 0.4028 -0.0187 0.0293 -0.0512 301 NAG A C8 3270 N N2 . NAG C . ? 0.4328 0.4526 0.4976 -0.0213 0.0317 -0.0542 301 NAG A N2 3271 O O3 . NAG C . ? 0.4038 0.4203 0.4694 -0.0220 0.0330 -0.0541 301 NAG A O3 3272 O O4 . NAG C . ? 0.5265 0.5456 0.5923 -0.0249 0.0360 -0.0584 301 NAG A O4 3273 O O5 . NAG C . ? 0.5362 0.5613 0.5990 -0.0258 0.0349 -0.0598 301 NAG A O5 3274 O O6 . NAG C . ? 0.7457 0.7691 0.8071 -0.0272 0.0358 -0.0603 301 NAG A O6 3275 O O7 . NAG C . ? 0.5216 0.5411 0.5841 -0.0208 0.0301 -0.0525 301 NAG A O7 3276 C C1 . NAG D . ? 0.5468 0.5637 0.6128 -0.0249 0.0362 -0.0577 302 NAG A C1 3277 C C2 . NAG D . ? 0.5570 0.5737 0.6243 -0.0256 0.0376 -0.0590 302 NAG A C2 3278 C C3 . NAG D . ? 0.6633 0.6778 0.7309 -0.0256 0.0379 -0.0583 302 NAG A C3 3279 C C4 . NAG D . ? 0.7287 0.7411 0.7964 -0.0244 0.0367 -0.0559 302 NAG A C4 3280 C C5 . NAG D . ? 0.6362 0.6491 0.7028 -0.0237 0.0353 -0.0548 302 NAG A C5 3281 C C6 . NAG D . ? 0.6173 0.6283 0.6845 -0.0224 0.0341 -0.0523 302 NAG A C6 3282 C C7 . NAG D . ? 0.5664 0.5873 0.6340 -0.0278 0.0395 -0.0627 302 NAG A C7 3283 C C8 . NAG D . ? 0.3816 0.4052 0.4483 -0.0296 0.0406 -0.0650 302 NAG A C8 3284 N N2 . NAG D . ? 0.6205 0.6397 0.6873 -0.0272 0.0387 -0.0613 302 NAG A N2 3285 O O3 . NAG D . ? 0.7157 0.7295 0.7848 -0.0258 0.0389 -0.0589 302 NAG A O3 3286 O O4 . NAG D . ? 1.0699 1.0815 1.1374 -0.0251 0.0372 -0.0560 302 NAG A O4 3287 O O5 . NAG D . ? 0.5950 0.6097 0.6615 -0.0235 0.0351 -0.0555 302 NAG A O5 3288 O O6 . NAG D . ? 0.8189 0.8298 0.8868 -0.0213 0.0334 -0.0516 302 NAG A O6 3289 O O7 . NAG D . ? 0.5994 0.6201 0.6686 -0.0269 0.0393 -0.0621 302 NAG A O7 3290 C C1 . BMA E . ? 1.0486 1.0580 1.1169 -0.0245 0.0368 -0.0543 303 BMA A C1 3291 C C2 . BMA E . ? 1.1256 1.1350 1.1936 -0.0252 0.0371 -0.0542 303 BMA A C2 3292 C C3 . BMA E . ? 1.1391 1.1467 1.2083 -0.0247 0.0369 -0.0525 303 BMA A C3 3293 C C4 . BMA E . ? 1.0991 1.1054 1.1694 -0.0245 0.0375 -0.0524 303 BMA A C4 3294 C C5 . BMA E . ? 1.0333 1.0396 1.1036 -0.0239 0.0372 -0.0527 303 BMA A C5 3295 C C6 . BMA E . ? 1.0200 1.0253 1.0916 -0.0239 0.0380 -0.0531 303 BMA A C6 3296 O O2 . BMA E . ? 1.2197 1.2298 1.2875 -0.0265 0.0384 -0.0562 303 BMA A O2 3297 O O3 . BMA E . ? 1.2780 1.2857 1.3472 -0.0254 0.0376 -0.0527 303 BMA A O3 3298 O O4 . BMA E . ? 1.0063 1.0112 1.0776 -0.0239 0.0371 -0.0505 303 BMA A O4 3299 O O5 . BMA E . ? 0.8874 0.8956 0.9569 -0.0245 0.0376 -0.0545 303 BMA A O5 3300 O O6 . BMA E . ? 1.0077 1.0128 1.0798 -0.0228 0.0374 -0.0524 303 BMA A O6 3301 C C1 . NAG F . ? 0.3786 0.3996 0.3372 -0.0017 -0.0184 0.0402 301 NAG B C1 3302 C C2 . NAG F . ? 0.3743 0.3820 0.3260 0.0022 -0.0184 0.0396 301 NAG B C2 3303 C C3 . NAG F . ? 0.3744 0.3826 0.3263 0.0022 -0.0173 0.0410 301 NAG B C3 3304 C C4 . NAG F . ? 0.3516 0.3670 0.3080 -0.0001 -0.0180 0.0422 301 NAG B C4 3305 C C5 . NAG F . ? 0.3866 0.4134 0.3488 -0.0032 -0.0177 0.0420 301 NAG B C5 3306 C C6 . NAG F . ? 0.4071 0.4415 0.3739 -0.0056 -0.0183 0.0430 301 NAG B C6 3307 C C7 . NAG F . ? 0.4757 0.4700 0.4200 0.0065 -0.0184 0.0377 301 NAG B C7 3308 C C8 . NAG F . ? 0.2827 0.2706 0.2230 0.0084 -0.0173 0.0368 301 NAG B C8 3309 N N2 . NAG F . ? 0.3511 0.3527 0.2991 0.0042 -0.0175 0.0388 301 NAG B N2 3310 O O3 . NAG F . ? 0.3909 0.3891 0.3376 0.0049 -0.0175 0.0414 301 NAG B O3 3311 O O4 . NAG F . ? 0.4523 0.4694 0.4095 -0.0003 -0.0169 0.0438 301 NAG B O4 3312 O O5 . NAG F . ? 0.4501 0.4773 0.4125 -0.0037 -0.0189 0.0411 301 NAG B O5 3313 O O6 . NAG F . ? 0.4332 0.4615 0.3977 -0.0045 -0.0199 0.0432 301 NAG B O6 3314 O O7 . NAG F . ? 0.5301 0.5236 0.4747 0.0070 -0.0199 0.0374 301 NAG B O7 3315 C C1 . NAG G . ? 0.4521 0.4648 0.4074 0.0006 -0.0179 0.0449 302 NAG B C1 3316 C C2 . NAG G . ? 0.4943 0.5128 0.4527 -0.0006 -0.0166 0.0466 302 NAG B C2 3317 C C3 . NAG G . ? 0.5475 0.5614 0.5039 0.0004 -0.0173 0.0478 302 NAG B C3 3318 C C4 . NAG G . ? 0.5189 0.5210 0.4687 0.0035 -0.0175 0.0472 302 NAG B C4 3319 C C5 . NAG G . ? 0.5876 0.5850 0.5349 0.0046 -0.0187 0.0455 302 NAG B C5 3320 C C6 . NAG G . ? 0.5834 0.5699 0.5246 0.0080 -0.0186 0.0448 302 NAG B C6 3321 C C7 . NAG G . ? 0.4976 0.5353 0.4659 -0.0049 -0.0146 0.0472 302 NAG B C7 3322 C C8 . NAG G . ? 0.3793 0.4130 0.3449 -0.0032 -0.0130 0.0471 302 NAG B C8 3323 N N2 . NAG G . ? 0.4450 0.4750 0.4096 -0.0036 -0.0163 0.0470 302 NAG B N2 3324 O O3 . NAG G . ? 0.5840 0.6032 0.5432 -0.0006 -0.0160 0.0494 302 NAG B O3 3325 O O4 . NAG G . ? 0.6994 0.6976 0.6474 0.0043 -0.0180 0.0482 302 NAG B O4 3326 O O5 . NAG G . ? 0.5303 0.5319 0.4796 0.0036 -0.0181 0.0445 302 NAG B O5 3327 O O6 . NAG G . ? 0.6312 0.6145 0.5701 0.0087 -0.0172 0.0449 302 NAG B O6 3328 O O7 . NAG G . ? 0.4648 0.5123 0.4384 -0.0074 -0.0143 0.0475 302 NAG B O7 3329 C C1 . BMA H . ? 0.6864 0.6780 0.6304 0.0061 -0.0170 0.0487 303 BMA B C1 3330 C C2 . BMA H . ? 0.7150 0.6998 0.6554 0.0078 -0.0179 0.0492 303 BMA B C2 3331 C C3 . BMA H . ? 0.8161 0.7971 0.7541 0.0086 -0.0169 0.0501 303 BMA B C3 3332 C C4 . BMA H . ? 0.8606 0.8508 0.8040 0.0063 -0.0161 0.0518 303 BMA B C4 3333 C C5 . BMA H . ? 0.8141 0.8143 0.7630 0.0042 -0.0154 0.0518 303 BMA B C5 3334 C C6 . BMA H . ? 0.8015 0.8114 0.7562 0.0017 -0.0161 0.0525 303 BMA B C6 3335 O O2 . BMA H . ? 0.7673 0.7575 0.7112 0.0062 -0.0189 0.0501 303 BMA B O2 3336 O O3 . BMA H . ? 0.7523 0.7255 0.6858 0.0108 -0.0173 0.0502 303 BMA B O3 3337 O O4 . BMA H . ? 0.9698 0.9571 0.9113 0.0070 -0.0150 0.0527 303 BMA B O4 3338 O O5 . BMA H . ? 0.8352 0.8328 0.7824 0.0048 -0.0156 0.0501 303 BMA B O5 3339 O O6 . BMA H . ? 0.6332 0.6492 0.5915 0.0006 -0.0152 0.0542 303 BMA B O6 3340 O O . HOH I . ? 0.8929 0.8428 0.8920 -0.0106 -0.0603 -0.0018 401 HOH A O 3341 O O . HOH I . ? 0.4763 0.5277 0.5372 -0.0285 0.0232 -0.0475 402 HOH A O 3342 O O . HOH I . ? 1.0061 1.0171 1.1337 -0.0239 0.0500 -0.0540 403 HOH A O 3343 O O . HOH I . ? 0.7635 0.7797 0.8736 -0.0326 0.0583 -0.0704 404 HOH A O 3344 O O . HOH I . ? 0.7286 0.7584 0.8553 -0.0335 0.0250 -0.0316 405 HOH A O 3345 O O . HOH I . ? 0.8551 0.7740 0.8349 0.0052 -0.0530 -0.0038 406 HOH A O 3346 O O . HOH I . ? 0.5021 0.5197 0.5743 -0.0227 0.0364 -0.0574 407 HOH A O 3347 O O . HOH I . ? 0.6722 0.6795 0.7749 -0.0201 0.0450 -0.0564 408 HOH A O 3348 O O . HOH I . ? 0.7303 0.6390 0.6866 0.0158 -0.0400 -0.0043 409 HOH A O 3349 O O . HOH I . ? 0.7085 0.7134 0.8472 -0.0328 0.0713 -0.0673 410 HOH A O 3350 O O . HOH I . ? 0.9302 0.9649 1.0541 -0.0429 0.0573 -0.0599 411 HOH A O 3351 O O . HOH I . ? 0.3323 0.3105 0.3758 0.0039 0.0131 -0.0349 412 HOH A O 3352 O O . HOH I . ? 1.0125 1.0172 1.1364 -0.0295 0.0642 -0.0695 413 HOH A O 3353 O O . HOH I . ? 0.7484 0.6463 0.6817 0.0295 -0.0222 -0.0083 414 HOH A O 3354 O O . HOH I . ? 0.7628 0.6630 0.7029 0.0272 -0.0250 -0.0084 415 HOH A O 3355 O O . HOH I . ? 0.5841 0.6118 0.6491 -0.0273 -0.0051 -0.0330 416 HOH A O 3356 O O . HOH I . ? 0.4736 0.4992 0.5740 -0.0333 0.0014 -0.0232 417 HOH A O 3357 O O . HOH I . ? 0.4365 0.4809 0.5066 -0.0276 0.0174 -0.0412 418 HOH A O 3358 O O . HOH I . ? 0.4470 0.4970 0.5345 -0.0390 0.0056 -0.0271 419 HOH A O 3359 O O . HOH I . ? 0.7637 0.7822 0.8574 -0.0426 0.0661 -0.0846 420 HOH A O 3360 O O . HOH I . ? 0.4371 0.4238 0.5008 -0.0027 0.0108 -0.0368 421 HOH A O 3361 O O . HOH I . ? 0.3436 0.2802 0.3293 0.0160 -0.0092 -0.0226 422 HOH A O 3362 O O . HOH I . ? 0.3505 0.3497 0.4271 -0.0140 0.0027 -0.0386 423 HOH A O 3363 O O . HOH I . ? 0.3103 0.3628 0.3928 -0.0359 0.0278 -0.0478 424 HOH A O 3364 O O . HOH I . ? 0.4216 0.3197 0.3503 0.0198 -0.0369 -0.0016 425 HOH A O 3365 O O . HOH I . ? 0.4948 0.4416 0.4888 0.0137 -0.0012 -0.0288 426 HOH A O 3366 O O . HOH I . ? 0.3862 0.4006 0.4669 -0.0129 0.0257 -0.0433 427 HOH A O 3367 O O . HOH I . ? 0.3131 0.3317 0.3908 -0.0190 0.0329 -0.0540 428 HOH A O 3368 O O . HOH I . ? 0.4136 0.4313 0.4753 -0.0201 0.0285 -0.0495 429 HOH A O 3369 O O . HOH I . ? 0.7895 0.8293 0.9055 -0.0401 0.0139 -0.0257 430 HOH A O 3370 O O . HOH I . ? 0.6668 0.5931 0.6381 0.0036 -0.0528 0.0009 431 HOH A O 3371 O O . HOH I . ? 0.7704 0.7329 0.7701 -0.0124 -0.0572 -0.0013 432 HOH A O 3372 O O . HOH I . ? 0.4111 0.4305 0.4810 -0.0199 0.0319 -0.0539 433 HOH A O 3373 O O . HOH I . ? 0.6428 0.6517 0.7536 -0.0184 0.0428 -0.0546 434 HOH A O 3374 O O . HOH I . ? 0.4866 0.5026 0.5723 -0.0223 0.0400 -0.0588 435 HOH A O 3375 O O . HOH I . ? 0.4637 0.4034 0.4851 0.0030 -0.0218 -0.0204 436 HOH A O 3376 O O . HOH I . ? 0.3543 0.3914 0.4351 -0.0279 0.0325 -0.0545 437 HOH A O 3377 O O . HOH I . ? 0.4528 0.5017 0.5200 -0.0300 0.0277 -0.0519 438 HOH A O 3378 O O . HOH I . ? 0.3957 0.4140 0.4574 -0.0114 0.0224 -0.0480 439 HOH A O 3379 O O . HOH I . ? 0.4802 0.4807 0.5173 -0.0221 -0.0331 -0.0215 440 HOH A O 3380 O O . HOH I . ? 0.6016 0.6556 0.6609 -0.0398 0.0406 -0.0719 441 HOH A O 3381 O O . HOH I . ? 0.4848 0.4563 0.5335 0.0018 0.0055 -0.0325 442 HOH A O 3382 O O . HOH I . ? 0.6717 0.7272 0.7488 -0.0401 0.0387 -0.0612 443 HOH A O 3383 O O . HOH I . ? 0.6891 0.6303 0.6553 0.0087 -0.0342 -0.0027 444 HOH A O 3384 O O . HOH I . ? 0.4034 0.4208 0.4792 -0.0150 0.0259 -0.0448 445 HOH A O 3385 O O . HOH I . ? 0.5232 0.4593 0.5353 0.0080 -0.0108 -0.0215 446 HOH A O 3386 O O . HOH I . ? 0.5361 0.5846 0.6004 -0.0277 0.0181 -0.0420 447 HOH A O 3387 O O . HOH I . ? 0.4642 0.4585 0.5072 0.0004 0.0219 -0.0381 448 HOH A O 3388 O O . HOH I . ? 0.5697 0.5836 0.6756 -0.0212 0.0128 -0.0321 449 HOH A O 3389 O O . HOH I . ? 0.4768 0.5179 0.5435 -0.0244 0.0177 -0.0442 450 HOH A O 3390 O O . HOH I . ? 0.4439 0.4287 0.4666 0.0082 0.0212 -0.0346 451 HOH A O 3391 O O . HOH I . ? 0.4960 0.4571 0.5381 0.0034 0.0004 -0.0296 452 HOH A O 3392 O O . HOH I . ? 0.5434 0.5563 0.6630 -0.0181 0.0293 -0.0403 453 HOH A O 3393 O O . HOH I . ? 0.5586 0.5813 0.6174 -0.0125 0.0225 -0.0498 454 HOH A O 3394 O O . HOH I . ? 0.7451 0.6463 0.6775 0.0179 -0.0378 0.0000 455 HOH A O 3395 O O . HOH I . ? 0.6723 0.7291 0.7449 -0.0425 0.0424 -0.0675 456 HOH A O 3396 O O . HOH I . ? 0.7597 0.6799 0.7545 0.0120 -0.0327 -0.0110 457 HOH A O 3397 O O . HOH I . ? 0.6450 0.5443 0.5839 0.0092 -0.0538 0.0012 458 HOH A O 3398 O O . HOH I . ? 0.3821 0.4261 0.4694 -0.0382 0.0014 -0.0244 459 HOH A O 3399 O O . HOH I . ? 1.1123 1.1602 1.2020 -0.0509 0.0602 -0.0805 460 HOH A O 3400 O O . HOH I . ? 0.6553 0.5741 0.6366 0.0038 -0.0577 -0.0021 461 HOH A O 3401 O O . HOH I . ? 0.5213 0.5108 0.5930 -0.0039 0.0117 -0.0366 462 HOH A O 3402 O O . HOH I . ? 0.7631 0.7606 0.9117 -0.0226 0.0639 -0.0559 463 HOH A O 3403 O O . HOH I . ? 0.5982 0.6302 0.6473 -0.0339 -0.0259 -0.0193 464 HOH A O 3404 O O . HOH I . ? 0.3683 0.3829 0.4390 -0.0172 0.0301 -0.0498 465 HOH A O 3405 O O . HOH I . ? 0.6409 0.5614 0.6042 0.0047 -0.0563 0.0055 466 HOH A O 3406 O O . HOH I . ? 0.5770 0.4735 0.5144 0.0267 -0.0294 -0.0081 467 HOH A O 3407 O O . HOH I . ? 0.5860 0.6023 0.6645 -0.0242 0.0405 -0.0602 468 HOH A O 3408 O O . HOH I . ? 0.7931 0.8120 0.8388 -0.0291 -0.0303 -0.0208 469 HOH A O 3409 O O . HOH I . ? 0.6437 0.5375 0.5743 0.0106 -0.0533 0.0010 470 HOH A O 3410 O O . HOH I . ? 0.5398 0.4577 0.5228 0.0061 -0.0536 -0.0032 471 HOH A O 3411 O O . HOH I . ? 0.7321 0.6431 0.7124 0.0108 -0.0500 -0.0056 472 HOH A O 3412 O O . HOH J . ? 0.9118 1.0812 0.9532 -0.0015 -0.0012 0.0823 401 HOH B O 3413 O O . HOH J . ? 0.6598 0.6175 0.6609 0.0146 0.0135 -0.0262 402 HOH B O 3414 O O . HOH J . ? 0.5783 0.7578 0.6121 -0.0074 -0.0047 0.0753 403 HOH B O 3415 O O . HOH J . ? 0.6140 0.5571 0.5884 0.0251 0.0076 -0.0164 404 HOH B O 3416 O O . HOH J . ? 0.6326 0.7836 0.6630 -0.0106 -0.0048 0.0685 405 HOH B O 3417 O O . HOH J . ? 0.4809 0.3997 0.4058 0.0287 -0.0058 0.0077 406 HOH B O 3418 O O . HOH J . ? 0.5233 0.4801 0.4662 0.0158 -0.0129 0.0372 407 HOH B O 3419 O O . HOH J . ? 0.5790 0.4756 0.5094 0.0234 -0.0341 -0.0050 408 HOH B O 3420 O O . HOH J . ? 0.6636 0.8335 0.6966 -0.0135 -0.0080 0.0706 409 HOH B O 3421 O O . HOH J . ? 0.7425 0.7122 0.7389 0.0214 0.0113 -0.0290 410 HOH B O 3422 O O . HOH J . ? 0.3834 0.4232 0.3528 -0.0083 -0.0207 0.0409 411 HOH B O 3423 O O . HOH J . ? 0.7684 0.7276 0.7122 0.0326 0.0210 -0.0013 412 HOH B O 3424 O O . HOH J . ? 0.4915 0.4997 0.4844 0.0123 0.0262 -0.0268 413 HOH B O 3425 O O . HOH J . ? 0.6449 0.6673 0.6075 -0.0009 -0.0153 0.0569 414 HOH B O 3426 O O . HOH J . ? 0.5270 0.5265 0.4679 0.0153 0.0057 0.0274 415 HOH B O 3427 O O . HOH J . ? 0.6022 0.7767 0.6316 -0.0124 -0.0071 0.0689 416 HOH B O 3428 O O . HOH J . ? 0.3773 0.4576 0.3628 -0.0031 0.0095 0.0369 417 HOH B O 3429 O O . HOH J . ? 0.6361 0.5855 0.6120 0.0246 0.0103 -0.0172 418 HOH B O 3430 O O . HOH J . ? 0.6541 0.6037 0.6272 0.0258 0.0131 -0.0160 419 HOH B O 3431 O O . HOH J . ? 0.6854 0.8509 0.7069 -0.0129 -0.0057 0.0595 420 HOH B O 3432 O O . HOH J . ? 0.4763 0.4769 0.4236 0.0073 -0.0019 0.0449 421 HOH B O 3433 O O . HOH J . ? 0.4388 0.4055 0.3857 0.0234 0.0062 0.0001 422 HOH B O 3434 O O . HOH J . ? 0.3567 0.3294 0.2956 0.0167 -0.0045 0.0298 423 HOH B O 3435 O O . HOH J . ? 0.4915 0.5083 0.4532 -0.0045 -0.0259 0.0235 424 HOH B O 3436 O O . HOH J . ? 0.3990 0.3956 0.3467 0.0120 0.0062 0.0384 425 HOH B O 3437 O O . HOH J . ? 0.2448 0.3110 0.2223 -0.0063 -0.0018 0.0412 426 HOH B O 3438 O O . HOH J . ? 0.3424 0.3453 0.2895 0.0046 -0.0088 0.0416 427 HOH B O 3439 O O . HOH J . ? 0.5605 0.4420 0.4444 0.0331 -0.0160 -0.0019 428 HOH B O 3440 O O . HOH J . ? 0.4706 0.3872 0.4018 0.0287 -0.0078 -0.0009 429 HOH B O 3441 O O . HOH J . ? 0.6545 0.7900 0.6741 -0.0186 -0.0074 0.0550 430 HOH B O 3442 O O . HOH J . ? 0.6034 0.6588 0.5838 0.0119 0.0157 0.0514 431 HOH B O 3443 O O . HOH J . ? 0.4688 0.3771 0.4050 0.0153 -0.0369 0.0059 432 HOH B O 3444 O O . HOH J . ? 0.2502 0.3058 0.2270 -0.0073 -0.0100 0.0479 433 HOH B O 3445 O O . HOH J . ? 0.2736 0.3880 0.2731 -0.0155 -0.0005 0.0359 434 HOH B O 3446 O O . HOH J . ? 0.4410 0.4875 0.4103 -0.0017 0.0048 0.0113 435 HOH B O 3447 O O . HOH J . ? 0.4463 0.3879 0.3834 0.0204 -0.0113 0.0278 436 HOH B O 3448 O O . HOH J . ? 0.6278 0.7550 0.6484 -0.0030 0.0012 0.0709 437 HOH B O 3449 O O . HOH J . ? 0.4350 0.4612 0.3958 0.0099 0.0160 0.0338 438 HOH B O 3450 O O . HOH J . ? 0.3481 0.4522 0.3402 -0.0179 -0.0033 0.0341 439 HOH B O 3451 O O . HOH J . ? 0.5665 0.4959 0.4922 0.0335 0.0078 0.0056 440 HOH B O 3452 O O . HOH J . ? 0.7524 0.9097 0.7637 -0.0111 0.0003 0.0483 441 HOH B O 3453 O O . HOH J . ? 0.4262 0.4223 0.3748 0.0185 0.0149 0.0283 442 HOH B O 3454 O O . HOH J . ? 0.5044 0.6336 0.5089 -0.0052 0.0082 0.0440 443 HOH B O 3455 O O . HOH J . ? 0.4043 0.3234 0.3591 0.0223 -0.0204 -0.0080 444 HOH B O 3456 O O . HOH J . ? 0.4237 0.3441 0.3544 0.0292 -0.0043 0.0012 445 HOH B O 3457 O O . HOH J . ? 0.3331 0.4661 0.3423 -0.0212 -0.0067 0.0396 446 HOH B O 3458 O O . HOH J . ? 0.8617 0.8544 0.8059 0.0064 -0.0123 0.0522 447 HOH B O 3459 O O . HOH J . ? 0.4644 0.3977 0.4439 0.0247 0.0023 -0.0176 448 HOH B O 3460 O O . HOH J . ? 0.4290 0.5162 0.4240 0.0065 0.0127 0.0540 449 HOH B O 3461 O O . HOH J . ? 0.3161 0.4421 0.3207 -0.0197 -0.0044 0.0368 450 HOH B O 3462 O O . HOH J . ? 0.5054 0.6180 0.5129 -0.0221 -0.0100 0.0498 451 HOH B O 3463 O O . HOH J . ? 0.7671 0.8709 0.7578 -0.0228 -0.0086 0.0315 452 HOH B O 3464 O O . HOH J . ? 0.3658 0.3439 0.3032 0.0055 -0.0120 0.0360 453 HOH B O 3465 O O . HOH J . ? 0.3765 0.4078 0.3403 0.0020 -0.0035 0.0506 454 HOH B O 3466 O O . HOH J . ? 0.5696 0.6039 0.5382 -0.0064 -0.0203 0.0463 455 HOH B O 3467 O O . HOH J . ? 0.3361 0.3383 0.2832 0.0042 -0.0133 0.0394 456 HOH B O 3468 O O . HOH J . ? 0.3504 0.4216 0.3223 -0.0098 -0.0031 0.0299 457 HOH B O 3469 O O . HOH J . ? 0.4599 0.4749 0.4148 0.0018 -0.0116 0.0457 458 HOH B O 3470 O O . HOH J . ? 0.5166 0.5033 0.4610 0.0126 0.0031 0.0361 459 HOH B O 3471 O O . HOH J . ? 0.3876 0.5000 0.3871 -0.0132 0.0012 0.0368 460 HOH B O 3472 O O . HOH J . ? 0.5047 0.5353 0.4980 -0.0011 0.0125 -0.0208 461 HOH B O 3473 O O . HOH J . ? 0.6993 0.6727 0.6460 0.0289 0.0219 -0.0043 462 HOH B O 3474 O O . HOH J . ? 0.4636 0.3950 0.3954 0.0332 0.0079 0.0024 463 HOH B O 3475 O O . HOH J . ? 0.4844 0.4918 0.4382 0.0014 -0.0235 0.0382 464 HOH B O 3476 O O . HOH J . ? 0.2899 0.2992 0.2449 0.0130 0.0097 0.0445 465 HOH B O 3477 O O . HOH J . ? 0.4803 0.5111 0.4486 0.0139 0.0136 0.0517 466 HOH B O 3478 O O . HOH J . ? 0.4493 0.4777 0.4345 0.0032 0.0164 -0.0174 467 HOH B O 3479 O O . HOH J . ? 0.5545 0.4669 0.4627 0.0344 0.0039 0.0019 468 HOH B O 3480 O O . HOH J . ? 0.6107 0.4942 0.5028 0.0303 -0.0215 -0.0020 469 HOH B O 3481 O O . HOH J . ? 0.6546 0.7454 0.6487 -0.0151 0.0155 -0.0025 470 HOH B O 3482 O O . HOH J . ? 0.4693 0.4609 0.4139 0.0070 -0.0207 0.0415 471 HOH B O 3483 O O . HOH J . ? 0.4375 0.3909 0.3775 0.0213 -0.0036 0.0266 472 HOH B O 3484 O O . HOH J . ? 0.8939 1.0335 0.9071 -0.0018 0.0057 0.0565 473 HOH B O 3485 O O . HOH J . ? 0.5268 0.5672 0.5114 -0.0030 0.0081 -0.0082 474 HOH B O 3486 O O . HOH J . ? 0.2850 0.2714 0.2298 0.0127 -0.0200 0.0357 475 HOH B O 3487 O O . HOH J . ? 0.6914 0.8265 0.7008 -0.0080 0.0023 0.0486 476 HOH B O 3488 O O . HOH J . ? 0.3377 0.3031 0.2781 0.0252 0.0067 0.0062 477 HOH B O 3489 O O . HOH J . ? 0.4740 0.5019 0.4514 -0.0084 -0.0193 0.0091 478 HOH B O 3490 O O . HOH J . ? 0.6857 0.8570 0.7325 0.0071 0.0037 0.0897 479 HOH B O 3491 O O . HOH J . ? 0.4863 0.6283 0.4945 -0.0219 -0.0073 0.0390 480 HOH B O 3492 O O . HOH J . ? 0.3308 0.3602 0.2880 -0.0034 -0.0186 0.0319 481 HOH B O 3493 O O . HOH J . ? 0.3384 0.3824 0.3010 -0.0056 -0.0122 0.0275 482 HOH B O 3494 O O . HOH J . ? 0.4582 0.3715 0.4106 0.0235 -0.0205 -0.0072 483 HOH B O 3495 O O . HOH J . ? 0.4866 0.5205 0.4473 0.0059 0.0128 0.0319 484 HOH B O 3496 O O . HOH J . ? 0.5488 0.4637 0.4965 0.0204 -0.0296 -0.0009 485 HOH B O 3497 O O . HOH J . ? 0.5131 0.5108 0.4588 0.0051 -0.0142 0.0436 486 HOH B O 3498 O O . HOH J . ? 0.3908 0.5282 0.4059 -0.0204 -0.0077 0.0470 487 HOH B O 3499 O O . HOH J . ? 0.5252 0.5520 0.4915 0.0136 0.0120 0.0537 488 HOH B O 3500 O O . HOH J . ? 0.3919 0.5267 0.3984 -0.0234 -0.0074 0.0360 489 HOH B O 3501 O O . HOH J . ? 0.6701 0.5621 0.5865 0.0227 -0.0342 -0.0019 490 HOH B O 3502 O O . HOH J . ? 0.3790 0.3657 0.3264 0.0089 -0.0253 0.0340 491 HOH B O 3503 O O . HOH J . ? 0.4338 0.5695 0.4508 -0.0186 -0.0070 0.0508 492 HOH B O 3504 O O . HOH J . ? 0.5119 0.5395 0.4840 -0.0084 -0.0234 0.0163 493 HOH B O 3505 O O . HOH J . ? 0.5869 0.4782 0.4898 0.0288 -0.0206 -0.0010 494 HOH B O 3506 O O . HOH J . ? 0.5272 0.6647 0.5327 -0.0232 -0.0070 0.0350 495 HOH B O 3507 O O . HOH J . ? 0.6063 0.6512 0.6067 -0.0081 0.0091 -0.0197 496 HOH B O 3508 O O . HOH J . ? 0.6319 0.6198 0.5723 0.0071 -0.0123 0.0449 497 HOH B O 3509 O O . HOH J . ? 0.5034 0.4620 0.4853 0.0187 0.0131 -0.0260 498 HOH B O 3510 O O . HOH J . ? 0.4716 0.4691 0.4212 0.0134 0.0066 0.0452 499 HOH B O 3511 O O . HOH J . ? 0.5659 0.7170 0.5968 0.0079 0.0074 0.0780 500 HOH B O 3512 O O . HOH J . ? 0.5537 0.4345 0.4343 0.0345 -0.0143 -0.0024 501 HOH B O 3513 O O . HOH J . ? 0.6142 0.6604 0.5909 -0.0117 -0.0179 0.0164 502 HOH B O 3514 O O . HOH J . ? 0.3765 0.4682 0.3591 -0.0165 -0.0040 0.0296 503 HOH B O 3515 O O . HOH J . ? 0.5201 0.5717 0.4951 -0.0051 -0.0085 0.0501 504 HOH B O 3516 O O . HOH J . ? 0.5646 0.4764 0.5062 0.0126 -0.0402 0.0070 505 HOH B O 3517 O O . HOH J . ? 0.5707 0.4597 0.4906 0.0242 -0.0376 -0.0052 506 HOH B O 3518 O O . HOH J . ? 0.6040 0.5033 0.5307 0.0167 -0.0382 0.0038 507 HOH B O 3519 O O . HOH J . ? 1.0076 1.1008 1.0098 -0.0176 0.0164 -0.0078 508 HOH B O 3520 O O . HOH J . ? 0.7440 0.6457 0.6753 0.0161 -0.0392 0.0029 509 HOH B O 3521 O O . HOH J . ? 0.4890 0.6254 0.5156 0.0121 0.0117 0.0775 510 HOH B O 3522 O O . HOH J . ? 0.5962 0.4790 0.5077 0.0255 -0.0394 -0.0058 511 HOH B O # loop_ _pdbx_poly_seq_scheme.asym_id _pdbx_poly_seq_scheme.entity_id _pdbx_poly_seq_scheme.seq_id _pdbx_poly_seq_scheme.mon_id _pdbx_poly_seq_scheme.ndb_seq_num _pdbx_poly_seq_scheme.pdb_seq_num _pdbx_poly_seq_scheme.auth_seq_num _pdbx_poly_seq_scheme.pdb_mon_id _pdbx_poly_seq_scheme.auth_mon_id _pdbx_poly_seq_scheme.pdb_strand_id _pdbx_poly_seq_scheme.pdb_ins_code _pdbx_poly_seq_scheme.hetero A 1 1 PRO 1 0 0 PRO PRO A . n A 1 2 SER 2 1 1 SER SER A . n A 1 3 ILE 3 2 2 ILE ILE A . n A 1 4 ILE 4 3 3 ILE ILE A . n A 1 5 VAL 5 4 4 VAL VAL A . n A 1 6 GLU 6 5 5 GLU GLU A . n A 1 7 PRO 7 6 6 PRO PRO A . n A 1 8 HIS 8 7 7 HIS HIS A . n A 1 9 VAL 9 8 8 VAL VAL A . n A 1 10 THR 10 9 9 THR THR A . n A 1 11 ALA 11 10 10 ALA ALA A . n A 1 12 VAL 12 11 11 VAL VAL A . n A 1 13 TRP 13 12 12 TRP TRP A . n A 1 14 GLY 14 13 13 GLY GLY A . n A 1 15 LYS 15 14 14 LYS LYS A . n A 1 16 ASN 16 15 15 ASN ASN A . n A 1 17 VAL 17 16 16 VAL VAL A . n A 1 18 SER 18 17 17 SER SER A . n A 1 19 LEU 19 18 18 LEU LEU A . n A 1 20 LYS 20 19 19 LYS LYS A . n A 1 21 CYS 21 20 20 CYS CYS A . n A 1 22 LEU 22 21 21 LEU LEU A . n A 1 23 ILE 23 22 22 ILE ILE A . n A 1 24 GLU 24 23 23 GLU GLU A . n A 1 25 VAL 25 24 24 VAL VAL A . n A 1 26 ASN 26 25 25 ASN ASN A . n A 1 27 GLU 27 26 26 GLU GLU A . n A 1 28 THR 28 27 27 THR THR A . n A 1 29 ILE 29 28 28 ILE ILE A . n A 1 30 THR 30 29 29 THR THR A . n A 1 31 GLN 31 30 30 GLN GLN A . n A 1 32 ILE 32 31 31 ILE ILE A . n A 1 33 SER 33 32 32 SER SER A . n A 1 34 TRP 34 33 33 TRP TRP A . n A 1 35 GLU 35 34 34 GLU GLU A . n A 1 36 LYS 36 35 35 LYS LYS A . n A 1 37 ILE 37 36 36 ILE ILE A . n A 1 38 HIS 38 37 37 HIS HIS A . n A 1 39 GLY 39 38 38 GLY GLY A . n A 1 40 LYS 40 39 39 LYS LYS A . n A 1 41 SER 41 40 40 SER SER A . n A 1 42 THR 42 41 41 THR THR A . n A 1 43 GLN 43 42 42 GLN GLN A . n A 1 44 THR 44 43 43 THR THR A . n A 1 45 VAL 45 44 44 VAL VAL A . n A 1 46 ALA 46 45 45 ALA ALA A . n A 1 47 VAL 47 46 46 VAL VAL A . n A 1 48 HIS 48 47 47 HIS HIS A . n A 1 49 HIS 49 48 48 HIS HIS A . n A 1 50 PRO 50 49 49 PRO PRO A . n A 1 51 GLN 51 50 50 GLN GLN A . n A 1 52 TYR 52 51 51 TYR TYR A . n A 1 53 GLY 53 52 52 GLY GLY A . n A 1 54 PHE 54 53 53 PHE PHE A . n A 1 55 SER 55 54 54 SER SER A . n A 1 56 VAL 56 55 55 VAL VAL A . n A 1 57 GLN 57 56 56 GLN GLN A . n A 1 58 GLY 58 57 57 GLY GLY A . n A 1 59 ASP 59 58 58 ASP ASP A . n A 1 60 TYR 60 59 59 TYR TYR A . n A 1 61 GLN 61 60 60 GLN GLN A . n A 1 62 GLY 62 61 61 GLY GLY A . n A 1 63 ARG 63 62 62 ARG ARG A . n A 1 64 VAL 64 63 63 VAL VAL A . n A 1 65 LEU 65 64 64 LEU LEU A . n A 1 66 PHE 66 65 65 PHE PHE A . n A 1 67 LYS 67 66 66 LYS LYS A . n A 1 68 ASN 68 67 67 ASN ASN A . n A 1 69 TYR 69 68 68 TYR TYR A . n A 1 70 SER 70 69 69 SER SER A . n A 1 71 LEU 71 70 70 LEU LEU A . n A 1 72 ASN 72 71 71 ASN ASN A . n A 1 73 ASP 73 72 72 ASP ASP A . n A 1 74 ALA 74 73 73 ALA ALA A . n A 1 75 THR 75 74 74 THR THR A . n A 1 76 ILE 76 75 75 ILE ILE A . n A 1 77 THR 77 76 76 THR THR A . n A 1 78 LEU 78 77 77 LEU LEU A . n A 1 79 HIS 79 78 78 HIS HIS A . n A 1 80 ASN 80 79 79 ASN ASN A . n A 1 81 ILE 81 80 80 ILE ILE A . n A 1 82 GLY 82 81 81 GLY GLY A . n A 1 83 PHE 83 82 82 PHE PHE A . n A 1 84 SER 84 83 83 SER SER A . n A 1 85 ASP 85 84 84 ASP ASP A . n A 1 86 SER 86 85 85 SER SER A . n A 1 87 GLY 87 86 86 GLY GLY A . n A 1 88 LYS 88 87 87 LYS LYS A . n A 1 89 TYR 89 88 88 TYR TYR A . n A 1 90 ILE 90 89 89 ILE ILE A . n A 1 91 CYS 91 90 90 CYS CYS A . n A 1 92 LYS 92 91 91 LYS LYS A . n A 1 93 ALA 93 92 92 ALA ALA A . n A 1 94 VAL 94 93 93 VAL VAL A . n A 1 95 THR 95 94 94 THR THR A . n A 1 96 PHE 96 95 95 PHE PHE A . n A 1 97 PRO 97 96 96 PRO PRO A . n A 1 98 LEU 98 97 97 LEU LEU A . n A 1 99 GLY 99 98 98 GLY GLY A . n A 1 100 ASN 100 99 99 ASN ASN A . n A 1 101 ALA 101 100 100 ALA ALA A . n A 1 102 GLN 102 101 101 GLN GLN A . n A 1 103 SER 103 102 102 SER SER A . n A 1 104 SER 104 103 103 SER SER A . n A 1 105 THR 105 104 104 THR THR A . n A 1 106 THR 106 105 105 THR THR A . n A 1 107 VAL 107 106 106 VAL VAL A . n A 1 108 THR 108 107 107 THR THR A . n A 1 109 VAL 109 108 108 VAL VAL A . n A 1 110 LEU 110 109 109 LEU LEU A . n A 1 111 VAL 111 110 110 VAL VAL A . n A 1 112 GLU 112 111 111 GLU GLU A . n A 1 113 PRO 113 112 112 PRO PRO A . n A 1 114 THR 114 113 113 THR THR A . n A 1 115 VAL 115 114 114 VAL VAL A . n A 1 116 SER 116 115 115 SER SER A . n A 1 117 LEU 117 116 116 LEU LEU A . n A 1 118 ILE 118 117 117 ILE ILE A . n A 1 119 LYS 119 118 118 LYS LYS A . n A 1 120 GLY 120 119 119 GLY GLY A . n A 1 121 PRO 121 120 120 PRO PRO A . n A 1 122 ASP 122 121 121 ASP ASP A . n A 1 123 SER 123 122 122 SER SER A . n A 1 124 LEU 124 123 123 LEU LEU A . n A 1 125 ILE 125 124 124 ILE ILE A . n A 1 126 ASP 126 125 125 ASP ASP A . n A 1 127 GLY 127 126 126 GLY GLY A . n A 1 128 GLY 128 127 127 GLY GLY A . n A 1 129 ASN 129 128 128 ASN ASN A . n A 1 130 GLU 130 129 129 GLU GLU A . n A 1 131 THR 131 130 130 THR ALA A . n A 1 132 VAL 132 131 131 VAL VAL A . n A 1 133 ALA 133 132 132 ALA ALA A . n A 1 134 ALA 134 133 133 ALA ALA A . n A 1 135 VAL 135 134 134 VAL VAL A . n A 1 136 CYS 136 135 135 CYS CYS A . n A 1 137 VAL 137 136 136 VAL VAL A . n A 1 138 ALA 138 137 137 ALA ALA A . n A 1 139 ALA 139 138 138 ALA ALA A . n A 1 140 THR 140 139 139 THR THR A . n A 1 141 GLY 141 140 140 GLY GLY A . n A 1 142 LYS 142 141 141 LYS LYS A . n A 1 143 PRO 143 142 142 PRO PRO A . n A 1 144 VAL 144 143 143 VAL VAL A . n A 1 145 ALA 145 144 144 ALA ALA A . n A 1 146 GLN 146 145 145 GLN GLN A . n A 1 147 ILE 147 146 146 ILE ILE A . n A 1 148 ASP 148 147 147 ASP ASP A . n A 1 149 TRP 149 148 148 TRP TRP A . n A 1 150 GLU 150 149 149 GLU GLU A . n A 1 151 GLY 151 150 150 GLY GLY A . n A 1 152 ASP 152 151 151 ASP ASP A . n A 1 153 LEU 153 152 152 LEU LEU A . n A 1 154 GLY 154 153 153 GLY GLY A . n A 1 155 GLU 155 154 154 GLU GLU A . n A 1 156 MET 156 155 155 MET MET A . n A 1 157 GLU 157 156 156 GLU GLU A . n A 1 158 SER 158 157 157 SER SER A . n A 1 159 SER 159 158 158 SER SER A . n A 1 160 THR 160 159 159 THR THR A . n A 1 161 THR 161 160 160 THR THR A . n A 1 162 SER 162 161 161 SER SER A . n A 1 163 PHE 163 162 162 PHE PHE A . n A 1 164 PRO 164 163 163 PRO PRO A . n A 1 165 ASN 165 164 164 ASN ASN A . n A 1 166 GLU 166 165 165 GLU GLU A . n A 1 167 THR 167 166 166 THR THR A . n A 1 168 ALA 168 167 167 ALA ALA A . n A 1 169 THR 169 168 168 THR THR A . n A 1 170 ILE 170 169 169 ILE ILE A . n A 1 171 VAL 171 170 170 VAL VAL A . n A 1 172 SER 172 171 171 SER SER A . n A 1 173 GLN 173 172 172 GLN GLN A . n A 1 174 TYR 174 173 173 TYR TYR A . n A 1 175 LYS 175 174 174 LYS LYS A . n A 1 176 LEU 176 175 175 LEU LEU A . n A 1 177 PHE 177 176 176 PHE PHE A . n A 1 178 PRO 178 177 177 PRO PRO A . n A 1 179 THR 179 178 178 THR THR A . n A 1 180 ARG 180 179 179 ARG ARG A . n A 1 181 PHE 181 180 180 PHE PHE A . n A 1 182 ALA 182 181 181 ALA ALA A . n A 1 183 ARG 183 182 182 ARG ARG A . n A 1 184 GLY 184 183 183 GLY GLY A . n A 1 185 ARG 185 184 184 ARG ARG A . n A 1 186 ARG 186 185 185 ARG ARG A . n A 1 187 ILE 187 186 186 ILE ILE A . n A 1 188 THR 188 187 187 THR THR A . n A 1 189 CYS 189 188 188 CYS CYS A . n A 1 190 VAL 190 189 189 VAL VAL A . n A 1 191 VAL 191 190 190 VAL VAL A . n A 1 192 LYS 192 191 191 LYS LYS A . n A 1 193 HIS 193 192 192 HIS HIS A . n A 1 194 PRO 194 193 193 PRO PRO A . n A 1 195 ALA 195 194 194 ALA ALA A . n A 1 196 LEU 196 195 195 LEU LEU A . n A 1 197 GLU 197 196 196 GLU GLU A . n A 1 198 LYS 198 197 197 LYS LYS A . n A 1 199 ASP 199 198 198 ASP ASP A . n A 1 200 ILE 200 199 199 ILE ILE A . n A 1 201 ARG 201 200 200 ARG ARG A . n A 1 202 TYR 202 201 201 TYR TYR A . n A 1 203 SER 203 202 202 SER SER A . n A 1 204 PHE 204 203 203 PHE PHE A . n A 1 205 ILE 205 204 204 ILE ILE A . n A 1 206 LEU 206 205 205 LEU LEU A . n A 1 207 ASP 207 206 206 ASP ASP A . n A 1 208 ILE 208 207 207 ILE ILE A . n A 1 209 GLN 209 208 208 GLN GLN A . n A 1 210 HIS 210 209 ? ? ? A . n A 1 211 HIS 211 210 ? ? ? A . n B 1 1 PRO 1 0 0 PRO PRO B . n B 1 2 SER 2 1 1 SER SER B . n B 1 3 ILE 3 2 2 ILE ILE B . n B 1 4 ILE 4 3 3 ILE ILE B . n B 1 5 VAL 5 4 4 VAL VAL B . n B 1 6 GLU 6 5 5 GLU GLU B . n B 1 7 PRO 7 6 6 PRO PRO B . n B 1 8 HIS 8 7 7 HIS HIS B . n B 1 9 VAL 9 8 8 VAL VAL B . n B 1 10 THR 10 9 9 THR THR B . n B 1 11 ALA 11 10 10 ALA ALA B . n B 1 12 VAL 12 11 11 VAL VAL B . n B 1 13 TRP 13 12 12 TRP TRP B . n B 1 14 GLY 14 13 13 GLY GLY B . n B 1 15 LYS 15 14 14 LYS LYS B . n B 1 16 ASN 16 15 15 ASN ASN B . n B 1 17 VAL 17 16 16 VAL VAL B . n B 1 18 SER 18 17 17 SER SER B . n B 1 19 LEU 19 18 18 LEU LEU B . n B 1 20 LYS 20 19 19 LYS LYS B . n B 1 21 CYS 21 20 20 CYS CYS B . n B 1 22 LEU 22 21 21 LEU LEU B . n B 1 23 ILE 23 22 22 ILE ILE B . n B 1 24 GLU 24 23 23 GLU GLU B . n B 1 25 VAL 25 24 24 VAL VAL B . n B 1 26 ASN 26 25 25 ASN ASN B . n B 1 27 GLU 27 26 26 GLU GLU B . n B 1 28 THR 28 27 27 THR THR B . n B 1 29 ILE 29 28 28 ILE ILE B . n B 1 30 THR 30 29 29 THR THR B . n B 1 31 GLN 31 30 30 GLN GLN B . n B 1 32 ILE 32 31 31 ILE ILE B . n B 1 33 SER 33 32 32 SER SER B . n B 1 34 TRP 34 33 33 TRP TRP B . n B 1 35 GLU 35 34 34 GLU GLU B . n B 1 36 LYS 36 35 35 LYS LYS B . n B 1 37 ILE 37 36 36 ILE ILE B . n B 1 38 HIS 38 37 37 HIS HIS B . n B 1 39 GLY 39 38 38 GLY GLY B . n B 1 40 LYS 40 39 39 LYS LYS B . n B 1 41 SER 41 40 40 SER SER B . n B 1 42 THR 42 41 41 THR THR B . n B 1 43 GLN 43 42 42 GLN GLN B . n B 1 44 THR 44 43 43 THR THR B . n B 1 45 VAL 45 44 44 VAL VAL B . n B 1 46 ALA 46 45 45 ALA ALA B . n B 1 47 VAL 47 46 46 VAL VAL B . n B 1 48 HIS 48 47 47 HIS HIS B . n B 1 49 HIS 49 48 48 HIS HIS B . n B 1 50 PRO 50 49 49 PRO PRO B . n B 1 51 GLN 51 50 50 GLN GLN B . n B 1 52 TYR 52 51 51 TYR TYR B . n B 1 53 GLY 53 52 52 GLY GLY B . n B 1 54 PHE 54 53 53 PHE PHE B . n B 1 55 SER 55 54 54 SER SER B . n B 1 56 VAL 56 55 55 VAL VAL B . n B 1 57 GLN 57 56 56 GLN GLN B . n B 1 58 GLY 58 57 57 GLY GLY B . n B 1 59 ASP 59 58 58 ASP ASP B . n B 1 60 TYR 60 59 59 TYR TYR B . n B 1 61 GLN 61 60 60 GLN GLN B . n B 1 62 GLY 62 61 61 GLY GLY B . n B 1 63 ARG 63 62 62 ARG ARG B . n B 1 64 VAL 64 63 63 VAL VAL B . n B 1 65 LEU 65 64 64 LEU LEU B . n B 1 66 PHE 66 65 65 PHE PHE B . n B 1 67 LYS 67 66 66 LYS LYS B . n B 1 68 ASN 68 67 67 ASN ASN B . n B 1 69 TYR 69 68 68 TYR TYR B . n B 1 70 SER 70 69 69 SER SER B . n B 1 71 LEU 71 70 70 LEU LEU B . n B 1 72 ASN 72 71 71 ASN ASN B . n B 1 73 ASP 73 72 72 ASP ASP B . n B 1 74 ALA 74 73 73 ALA ALA B . n B 1 75 THR 75 74 74 THR THR B . n B 1 76 ILE 76 75 75 ILE ILE B . n B 1 77 THR 77 76 76 THR THR B . n B 1 78 LEU 78 77 77 LEU LEU B . n B 1 79 HIS 79 78 78 HIS HIS B . n B 1 80 ASN 80 79 79 ASN ASN B . n B 1 81 ILE 81 80 80 ILE ILE B . n B 1 82 GLY 82 81 81 GLY GLY B . n B 1 83 PHE 83 82 82 PHE PHE B . n B 1 84 SER 84 83 83 SER SER B . n B 1 85 ASP 85 84 84 ASP ASP B . n B 1 86 SER 86 85 85 SER SER B . n B 1 87 GLY 87 86 86 GLY GLY B . n B 1 88 LYS 88 87 87 LYS LYS B . n B 1 89 TYR 89 88 88 TYR TYR B . n B 1 90 ILE 90 89 89 ILE ILE B . n B 1 91 CYS 91 90 90 CYS CYS B . n B 1 92 LYS 92 91 91 LYS LYS B . n B 1 93 ALA 93 92 92 ALA ALA B . n B 1 94 VAL 94 93 93 VAL VAL B . n B 1 95 THR 95 94 94 THR THR B . n B 1 96 PHE 96 95 95 PHE PHE B . n B 1 97 PRO 97 96 96 PRO PRO B . n B 1 98 LEU 98 97 97 LEU LEU B . n B 1 99 GLY 99 98 98 GLY GLY B . n B 1 100 ASN 100 99 99 ASN ASN B . n B 1 101 ALA 101 100 100 ALA ALA B . n B 1 102 GLN 102 101 101 GLN GLN B . n B 1 103 SER 103 102 102 SER SER B . n B 1 104 SER 104 103 103 SER SER B . n B 1 105 THR 105 104 104 THR THR B . n B 1 106 THR 106 105 105 THR THR B . n B 1 107 VAL 107 106 106 VAL VAL B . n B 1 108 THR 108 107 107 THR THR B . n B 1 109 VAL 109 108 108 VAL VAL B . n B 1 110 LEU 110 109 109 LEU LEU B . n B 1 111 VAL 111 110 110 VAL VAL B . n B 1 112 GLU 112 111 111 GLU GLU B . n B 1 113 PRO 113 112 112 PRO PRO B . n B 1 114 THR 114 113 113 THR THR B . n B 1 115 VAL 115 114 114 VAL VAL B . n B 1 116 SER 116 115 115 SER SER B . n B 1 117 LEU 117 116 116 LEU LEU B . n B 1 118 ILE 118 117 117 ILE ILE B . n B 1 119 LYS 119 118 118 LYS LYS B . n B 1 120 GLY 120 119 119 GLY GLY B . n B 1 121 PRO 121 120 120 PRO PRO B . n B 1 122 ASP 122 121 121 ASP ASP B . n B 1 123 SER 123 122 122 SER SER B . n B 1 124 LEU 124 123 123 LEU LEU B . n B 1 125 ILE 125 124 124 ILE ILE B . n B 1 126 ASP 126 125 125 ASP ASP B . n B 1 127 GLY 127 126 126 GLY GLY B . n B 1 128 GLY 128 127 127 GLY GLY B . n B 1 129 ASN 129 128 128 ASN ASN B . n B 1 130 GLU 130 129 129 GLU GLU B . n B 1 131 THR 131 130 130 THR ALA B . n B 1 132 VAL 132 131 131 VAL VAL B . n B 1 133 ALA 133 132 132 ALA ALA B . n B 1 134 ALA 134 133 133 ALA ALA B . n B 1 135 VAL 135 134 134 VAL VAL B . n B 1 136 CYS 136 135 135 CYS CYS B . n B 1 137 VAL 137 136 136 VAL VAL B . n B 1 138 ALA 138 137 137 ALA ALA B . n B 1 139 ALA 139 138 138 ALA ALA B . n B 1 140 THR 140 139 139 THR THR B . n B 1 141 GLY 141 140 140 GLY GLY B . n B 1 142 LYS 142 141 141 LYS LYS B . n B 1 143 PRO 143 142 142 PRO PRO B . n B 1 144 VAL 144 143 143 VAL VAL B . n B 1 145 ALA 145 144 144 ALA ALA B . n B 1 146 GLN 146 145 145 GLN GLN B . n B 1 147 ILE 147 146 146 ILE ILE B . n B 1 148 ASP 148 147 147 ASP ASP B . n B 1 149 TRP 149 148 148 TRP TRP B . n B 1 150 GLU 150 149 149 GLU GLU B . n B 1 151 GLY 151 150 150 GLY GLY B . n B 1 152 ASP 152 151 151 ASP ASP B . n B 1 153 LEU 153 152 152 LEU LEU B . n B 1 154 GLY 154 153 153 GLY GLY B . n B 1 155 GLU 155 154 154 GLU GLU B . n B 1 156 MET 156 155 155 MET MET B . n B 1 157 GLU 157 156 156 GLU GLU B . n B 1 158 SER 158 157 157 SER SER B . n B 1 159 SER 159 158 158 SER SER B . n B 1 160 THR 160 159 159 THR THR B . n B 1 161 THR 161 160 160 THR THR B . n B 1 162 SER 162 161 161 SER SER B . n B 1 163 PHE 163 162 162 PHE PHE B . n B 1 164 PRO 164 163 163 PRO PRO B . n B 1 165 ASN 165 164 164 ASN ASN B . n B 1 166 GLU 166 165 165 GLU GLU B . n B 1 167 THR 167 166 166 THR THR B . n B 1 168 ALA 168 167 167 ALA ALA B . n B 1 169 THR 169 168 168 THR THR B . n B 1 170 ILE 170 169 169 ILE ILE B . n B 1 171 VAL 171 170 170 VAL VAL B . n B 1 172 SER 172 171 171 SER SER B . n B 1 173 GLN 173 172 172 GLN GLN B . n B 1 174 TYR 174 173 173 TYR TYR B . n B 1 175 LYS 175 174 174 LYS LYS B . n B 1 176 LEU 176 175 175 LEU LEU B . n B 1 177 PHE 177 176 176 PHE PHE B . n B 1 178 PRO 178 177 177 PRO PRO B . n B 1 179 THR 179 178 178 THR THR B . n B 1 180 ARG 180 179 179 ARG ARG B . n B 1 181 PHE 181 180 180 PHE PHE B . n B 1 182 ALA 182 181 181 ALA ALA B . n B 1 183 ARG 183 182 182 ARG ARG B . n B 1 184 GLY 184 183 183 GLY GLY B . n B 1 185 ARG 185 184 184 ARG ARG B . n B 1 186 ARG 186 185 185 ARG ARG B . n B 1 187 ILE 187 186 186 ILE ILE B . n B 1 188 THR 188 187 187 THR THR B . n B 1 189 CYS 189 188 188 CYS CYS B . n B 1 190 VAL 190 189 189 VAL VAL B . n B 1 191 VAL 191 190 190 VAL VAL B . n B 1 192 LYS 192 191 191 LYS LYS B . n B 1 193 HIS 193 192 192 HIS HIS B . n B 1 194 PRO 194 193 193 PRO PRO B . n B 1 195 ALA 195 194 194 ALA ALA B . n B 1 196 LEU 196 195 195 LEU LEU B . n B 1 197 GLU 197 196 196 GLU GLU B . n B 1 198 LYS 198 197 197 LYS LYS B . n B 1 199 ASP 199 198 198 ASP ASP B . n B 1 200 ILE 200 199 199 ILE ILE B . n B 1 201 ARG 201 200 200 ARG ARG B . n B 1 202 TYR 202 201 201 TYR TYR B . n B 1 203 SER 203 202 202 SER SER B . n B 1 204 PHE 204 203 203 PHE PHE B . n B 1 205 ILE 205 204 204 ILE ILE B . n B 1 206 LEU 206 205 205 LEU LEU B . n B 1 207 ASP 207 206 206 ASP ASP B . n B 1 208 ILE 208 207 207 ILE ILE B . n B 1 209 GLN 209 208 208 GLN GLN B . n B 1 210 HIS 210 209 209 HIS HIS B . n B 1 211 HIS 211 210 210 HIS HIS B . n # loop_ _pdbx_nonpoly_scheme.asym_id _pdbx_nonpoly_scheme.entity_id _pdbx_nonpoly_scheme.mon_id _pdbx_nonpoly_scheme.ndb_seq_num _pdbx_nonpoly_scheme.pdb_seq_num _pdbx_nonpoly_scheme.auth_seq_num _pdbx_nonpoly_scheme.pdb_mon_id _pdbx_nonpoly_scheme.auth_mon_id _pdbx_nonpoly_scheme.pdb_strand_id _pdbx_nonpoly_scheme.pdb_ins_code C 2 NAG 1 301 4 NAG NAG A . D 2 NAG 2 302 5 NAG NAG A . E 3 BMA 3 303 6 BMA BMA A . F 2 NAG 1 301 1 NAG NAG B . G 2 NAG 2 302 2 NAG NAG B . H 3 BMA 3 303 3 BMA BMA B . I 4 HOH 1 401 87 HOH HOH A . I 4 HOH 2 402 168 HOH HOH A . I 4 HOH 3 403 51 HOH HOH A . I 4 HOH 4 404 85 HOH HOH A . I 4 HOH 5 405 109 HOH HOH A . I 4 HOH 6 406 113 HOH HOH A . I 4 HOH 7 407 186 HOH HOH A . I 4 HOH 8 408 71 HOH HOH A . I 4 HOH 9 409 178 HOH HOH A . I 4 HOH 10 410 122 HOH HOH A . I 4 HOH 11 411 132 HOH HOH A . I 4 HOH 12 412 2 HOH HOH A . I 4 HOH 13 413 192 HOH HOH A . I 4 HOH 14 414 146 HOH HOH A . I 4 HOH 15 415 90 HOH HOH A . I 4 HOH 16 416 144 HOH HOH A . I 4 HOH 17 417 94 HOH HOH A . I 4 HOH 18 418 52 HOH HOH A . I 4 HOH 19 419 159 HOH HOH A . I 4 HOH 20 420 74 HOH HOH A . I 4 HOH 21 421 39 HOH HOH A . I 4 HOH 22 422 73 HOH HOH A . I 4 HOH 23 423 1 HOH HOH A . I 4 HOH 24 424 6 HOH HOH A . I 4 HOH 25 425 46 HOH HOH A . I 4 HOH 26 426 105 HOH HOH A . I 4 HOH 27 427 50 HOH HOH A . I 4 HOH 28 428 3 HOH HOH A . I 4 HOH 29 429 34 HOH HOH A . I 4 HOH 30 430 133 HOH HOH A . I 4 HOH 31 431 198 HOH HOH A . I 4 HOH 32 432 129 HOH HOH A . I 4 HOH 33 433 29 HOH HOH A . I 4 HOH 34 434 55 HOH HOH A . I 4 HOH 35 435 4 HOH HOH A . I 4 HOH 36 436 76 HOH HOH A . I 4 HOH 37 437 5 HOH HOH A . I 4 HOH 38 438 30 HOH HOH A . I 4 HOH 39 439 170 HOH HOH A . I 4 HOH 40 440 67 HOH HOH A . I 4 HOH 41 441 63 HOH HOH A . I 4 HOH 42 442 66 HOH HOH A . I 4 HOH 43 443 83 HOH HOH A . I 4 HOH 44 444 81 HOH HOH A . I 4 HOH 45 445 28 HOH HOH A . I 4 HOH 46 446 148 HOH HOH A . I 4 HOH 47 447 130 HOH HOH A . I 4 HOH 48 448 108 HOH HOH A . I 4 HOH 49 449 196 HOH HOH A . I 4 HOH 50 450 42 HOH HOH A . I 4 HOH 51 451 56 HOH HOH A . I 4 HOH 52 452 179 HOH HOH A . I 4 HOH 53 453 48 HOH HOH A . I 4 HOH 54 454 193 HOH HOH A . I 4 HOH 55 455 153 HOH HOH A . I 4 HOH 56 456 115 HOH HOH A . I 4 HOH 57 457 184 HOH HOH A . I 4 HOH 58 458 152 HOH HOH A . I 4 HOH 59 459 175 HOH HOH A . I 4 HOH 60 460 197 HOH HOH A . I 4 HOH 61 461 149 HOH HOH A . I 4 HOH 62 462 194 HOH HOH A . I 4 HOH 63 463 195 HOH HOH A . I 4 HOH 64 464 180 HOH HOH A . I 4 HOH 65 465 126 HOH HOH A . I 4 HOH 66 466 181 HOH HOH A . I 4 HOH 67 467 100 HOH HOH A . I 4 HOH 68 468 117 HOH HOH A . I 4 HOH 69 469 176 HOH HOH A . I 4 HOH 70 470 135 HOH HOH A . I 4 HOH 71 471 99 HOH HOH A . I 4 HOH 72 472 58 HOH HOH A . J 4 HOH 1 401 121 HOH HOH B . J 4 HOH 2 402 116 HOH HOH B . J 4 HOH 3 403 78 HOH HOH B . J 4 HOH 4 404 187 HOH HOH B . J 4 HOH 5 405 54 HOH HOH B . J 4 HOH 6 406 86 HOH HOH B . J 4 HOH 7 407 61 HOH HOH B . J 4 HOH 8 408 41 HOH HOH B . J 4 HOH 9 409 169 HOH HOH B . J 4 HOH 10 410 96 HOH HOH B . J 4 HOH 11 411 37 HOH HOH B . J 4 HOH 12 412 91 HOH HOH B . J 4 HOH 13 413 38 HOH HOH B . J 4 HOH 14 414 114 HOH HOH B . J 4 HOH 15 415 80 HOH HOH B . J 4 HOH 16 416 69 HOH HOH B . J 4 HOH 17 417 21 HOH HOH B . J 4 HOH 18 418 77 HOH HOH B . J 4 HOH 19 419 123 HOH HOH B . J 4 HOH 20 420 47 HOH HOH B . J 4 HOH 21 421 18 HOH HOH B . J 4 HOH 22 422 7 HOH HOH B . J 4 HOH 23 423 9 HOH HOH B . J 4 HOH 24 424 59 HOH HOH B . J 4 HOH 25 425 19 HOH HOH B . J 4 HOH 26 426 12 HOH HOH B . J 4 HOH 27 427 11 HOH HOH B . J 4 HOH 28 428 155 HOH HOH B . J 4 HOH 29 429 15 HOH HOH B . J 4 HOH 30 430 158 HOH HOH B . J 4 HOH 31 431 24 HOH HOH B . J 4 HOH 32 432 102 HOH HOH B . J 4 HOH 33 433 112 HOH HOH B . J 4 HOH 34 434 13 HOH HOH B . J 4 HOH 35 435 111 HOH HOH B . J 4 HOH 36 436 62 HOH HOH B . J 4 HOH 37 437 64 HOH HOH B . J 4 HOH 38 438 20 HOH HOH B . J 4 HOH 39 439 156 HOH HOH B . J 4 HOH 40 440 44 HOH HOH B . J 4 HOH 41 441 143 HOH HOH B . J 4 HOH 42 442 23 HOH HOH B . J 4 HOH 43 443 145 HOH HOH B . J 4 HOH 44 444 120 HOH HOH B . J 4 HOH 45 445 16 HOH HOH B . J 4 HOH 46 446 92 HOH HOH B . J 4 HOH 47 447 139 HOH HOH B . J 4 HOH 48 448 84 HOH HOH B . J 4 HOH 49 449 65 HOH HOH B . J 4 HOH 50 450 45 HOH HOH B . J 4 HOH 51 451 70 HOH HOH B . J 4 HOH 52 452 88 HOH HOH B . J 4 HOH 53 453 10 HOH HOH B . J 4 HOH 54 454 17 HOH HOH B . J 4 HOH 55 455 53 HOH HOH B . J 4 HOH 56 456 75 HOH HOH B . J 4 HOH 57 457 32 HOH HOH B . J 4 HOH 58 458 157 HOH HOH B . J 4 HOH 59 459 104 HOH HOH B . J 4 HOH 60 460 14 HOH HOH B . J 4 HOH 61 461 107 HOH HOH B . J 4 HOH 62 462 101 HOH HOH B . J 4 HOH 63 463 172 HOH HOH B . J 4 HOH 64 464 22 HOH HOH B . J 4 HOH 65 465 36 HOH HOH B . J 4 HOH 66 466 154 HOH HOH B . J 4 HOH 67 467 31 HOH HOH B . J 4 HOH 68 468 182 HOH HOH B . J 4 HOH 69 469 43 HOH HOH B . J 4 HOH 70 470 140 HOH HOH B . J 4 HOH 71 471 27 HOH HOH B . J 4 HOH 72 472 97 HOH HOH B . J 4 HOH 73 473 131 HOH HOH B . J 4 HOH 74 474 33 HOH HOH B . J 4 HOH 75 475 103 HOH HOH B . J 4 HOH 76 476 151 HOH HOH B . J 4 HOH 77 477 8 HOH HOH B . J 4 HOH 78 478 25 HOH HOH B . J 4 HOH 79 479 79 HOH HOH B . J 4 HOH 80 480 35 HOH HOH B . J 4 HOH 81 481 167 HOH HOH B . J 4 HOH 82 482 183 HOH HOH B . J 4 HOH 83 483 60 HOH HOH B . J 4 HOH 84 484 138 HOH HOH B . J 4 HOH 85 485 26 HOH HOH B . J 4 HOH 86 486 89 HOH HOH B . J 4 HOH 87 487 124 HOH HOH B . J 4 HOH 88 488 163 HOH HOH B . J 4 HOH 89 489 93 HOH HOH B . J 4 HOH 90 490 173 HOH HOH B . J 4 HOH 91 491 160 HOH HOH B . J 4 HOH 92 492 127 HOH HOH B . J 4 HOH 93 493 191 HOH HOH B . J 4 HOH 94 494 165 HOH HOH B . J 4 HOH 95 495 119 HOH HOH B . J 4 HOH 96 496 110 HOH HOH B . J 4 HOH 97 497 189 HOH HOH B . J 4 HOH 98 498 141 HOH HOH B . J 4 HOH 99 499 136 HOH HOH B . J 4 HOH 100 500 72 HOH HOH B . J 4 HOH 101 501 171 HOH HOH B . J 4 HOH 102 502 188 HOH HOH B . J 4 HOH 103 503 137 HOH HOH B . J 4 HOH 104 504 118 HOH HOH B . J 4 HOH 105 505 95 HOH HOH B . J 4 HOH 106 506 82 HOH HOH B . J 4 HOH 107 507 162 HOH HOH B . J 4 HOH 108 508 190 HOH HOH B . J 4 HOH 109 509 147 HOH HOH B . J 4 HOH 110 510 68 HOH HOH B . J 4 HOH 111 511 177 HOH HOH B . # _pdbx_struct_assembly.id 1 _pdbx_struct_assembly.details author_defined_assembly _pdbx_struct_assembly.method_details ? _pdbx_struct_assembly.oligomeric_details dimeric _pdbx_struct_assembly.oligomeric_count 2 # _pdbx_struct_assembly_gen.assembly_id 1 _pdbx_struct_assembly_gen.oper_expression 1 _pdbx_struct_assembly_gen.asym_id_list A,B,C,D,E,F,G,H,I,J # loop_ _pdbx_struct_assembly_prop.biol_id _pdbx_struct_assembly_prop.type _pdbx_struct_assembly_prop.value _pdbx_struct_assembly_prop.details 1 'ABSA (A^2)' 2900 ? 1 MORE 8 ? 1 'SSA (A^2)' 22330 ? # _pdbx_struct_oper_list.id 1 _pdbx_struct_oper_list.type 'identity operation' _pdbx_struct_oper_list.name 1_555 _pdbx_struct_oper_list.symmetry_operation x,y,z _pdbx_struct_oper_list.matrix[1][1] 1.0000000000 _pdbx_struct_oper_list.matrix[1][2] 0.0000000000 _pdbx_struct_oper_list.matrix[1][3] 0.0000000000 _pdbx_struct_oper_list.vector[1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][2] 1.0000000000 _pdbx_struct_oper_list.matrix[2][3] 0.0000000000 _pdbx_struct_oper_list.vector[2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][1] 0.0000000000 _pdbx_struct_oper_list.matrix[3][2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][3] 1.0000000000 _pdbx_struct_oper_list.vector[3] 0.0000000000 # _pdbx_audit_revision_history.ordinal 1 _pdbx_audit_revision_history.data_content_type 'Structure model' _pdbx_audit_revision_history.major_revision 1 _pdbx_audit_revision_history.minor_revision 0 _pdbx_audit_revision_history.revision_date 2016-12-28 # _pdbx_audit_revision_details.ordinal 1 _pdbx_audit_revision_details.revision_ordinal 1 _pdbx_audit_revision_details.data_content_type 'Structure model' _pdbx_audit_revision_details.provider repository _pdbx_audit_revision_details.type 'Initial release' _pdbx_audit_revision_details.description ? # _pdbx_refine_tls.pdbx_refine_id 'X-RAY DIFFRACTION' _pdbx_refine_tls.id 1 _pdbx_refine_tls.details ? _pdbx_refine_tls.method refined _pdbx_refine_tls.origin_x 20.0830 _pdbx_refine_tls.origin_y 0.3810 _pdbx_refine_tls.origin_z 18.7608 _pdbx_refine_tls.T[1][1] 0.0724 _pdbx_refine_tls.T[2][2] 0.0958 _pdbx_refine_tls.T[3][3] 0.0832 _pdbx_refine_tls.T[1][2] -0.0112 _pdbx_refine_tls.T[1][3] -0.0062 _pdbx_refine_tls.T[2][3] -0.0228 _pdbx_refine_tls.L[1][1] 0.0108 _pdbx_refine_tls.L[2][2] 0.0329 _pdbx_refine_tls.L[3][3] -0.0139 _pdbx_refine_tls.L[1][2] 0.0191 _pdbx_refine_tls.L[1][3] -0.0627 _pdbx_refine_tls.L[2][3] -0.0424 _pdbx_refine_tls.S[1][1] -0.1006 _pdbx_refine_tls.S[1][2] 0.1412 _pdbx_refine_tls.S[1][3] -0.0211 _pdbx_refine_tls.S[2][1] 0.0959 _pdbx_refine_tls.S[2][2] 0.0534 _pdbx_refine_tls.S[2][3] -0.0529 _pdbx_refine_tls.S[3][1] -0.0568 _pdbx_refine_tls.S[3][2] -0.0149 _pdbx_refine_tls.S[3][3] -0.0000 # _pdbx_refine_tls_group.pdbx_refine_id 'X-RAY DIFFRACTION' _pdbx_refine_tls_group.id 1 _pdbx_refine_tls_group.refine_tls_id 1 _pdbx_refine_tls_group.beg_auth_asym_id ? _pdbx_refine_tls_group.beg_auth_seq_id ? _pdbx_refine_tls_group.beg_label_asym_id ? _pdbx_refine_tls_group.beg_label_seq_id ? _pdbx_refine_tls_group.end_auth_asym_id ? _pdbx_refine_tls_group.end_auth_seq_id ? _pdbx_refine_tls_group.end_label_asym_id ? _pdbx_refine_tls_group.end_label_seq_id ? _pdbx_refine_tls_group.selection ? _pdbx_refine_tls_group.selection_details all # loop_ _software.citation_id _software.classification _software.compiler_name _software.compiler_version _software.contact_author _software.contact_author_email _software.date _software.description _software.dependencies _software.hardware _software.language _software.location _software.mods _software.name _software.os _software.os_version _software.type _software.version _software.pdbx_ordinal ? refinement ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? '(1.10.1_2155: ???)' 1 ? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? iMOSFLM ? ? ? . 2 ? 'data scaling' ? ? ? ? ? ? ? ? ? ? ? SCALA ? ? ? . 3 # loop_ _pdbx_validate_close_contact.id _pdbx_validate_close_contact.PDB_model_num _pdbx_validate_close_contact.auth_atom_id_1 _pdbx_validate_close_contact.auth_asym_id_1 _pdbx_validate_close_contact.auth_comp_id_1 _pdbx_validate_close_contact.auth_seq_id_1 _pdbx_validate_close_contact.PDB_ins_code_1 _pdbx_validate_close_contact.label_alt_id_1 _pdbx_validate_close_contact.auth_atom_id_2 _pdbx_validate_close_contact.auth_asym_id_2 _pdbx_validate_close_contact.auth_comp_id_2 _pdbx_validate_close_contact.auth_seq_id_2 _pdbx_validate_close_contact.PDB_ins_code_2 _pdbx_validate_close_contact.label_alt_id_2 _pdbx_validate_close_contact.dist 1 1 NE2 B GLN 208 ? ? O B HOH 401 ? ? 1.57 2 1 O B LEU 123 ? ? OE1 B GLN 208 ? ? 1.63 3 1 O B GLN 208 ? ? O B HOH 401 ? ? 1.82 4 1 OE2 B GLU 26 ? ? O B HOH 402 ? ? 1.94 5 1 O A PRO 0 ? ? O A HOH 401 ? ? 1.98 6 1 C B LEU 123 ? ? OE1 B GLN 208 ? ? 2.06 7 1 OE2 A GLU 165 ? ? O A HOH 402 ? ? 2.07 8 1 O A ILE 204 ? ? O A HOH 403 ? ? 2.10 9 1 O A ILE 22 ? ? ND2 A ASN 71 ? ? 2.11 10 1 O A VAL 131 ? ? O A HOH 404 ? ? 2.11 11 1 O A ARG 185 ? ? O A HOH 405 ? ? 2.11 12 1 OD1 B ASP 125 ? ? O B HOH 403 ? ? 2.17 13 1 O A SER 1 ? ? O A HOH 406 ? ? 2.17 14 1 OG1 A THR 139 ? ? O A HOH 407 ? ? 2.18 15 1 N B LEU 97 ? ? O B HOH 402 ? ? 2.18 16 1 O B HOH 428 ? ? O B HOH 501 ? ? 2.19 # _pdbx_validate_symm_contact.id 1 _pdbx_validate_symm_contact.PDB_model_num 1 _pdbx_validate_symm_contact.auth_atom_id_1 NH1 _pdbx_validate_symm_contact.auth_asym_id_1 A _pdbx_validate_symm_contact.auth_comp_id_1 ARG _pdbx_validate_symm_contact.auth_seq_id_1 184 _pdbx_validate_symm_contact.PDB_ins_code_1 ? _pdbx_validate_symm_contact.label_alt_id_1 ? _pdbx_validate_symm_contact.site_symmetry_1 1_555 _pdbx_validate_symm_contact.auth_atom_id_2 O _pdbx_validate_symm_contact.auth_asym_id_2 B _pdbx_validate_symm_contact.auth_comp_id_2 HOH _pdbx_validate_symm_contact.auth_seq_id_2 508 _pdbx_validate_symm_contact.PDB_ins_code_2 ? _pdbx_validate_symm_contact.label_alt_id_2 ? _pdbx_validate_symm_contact.site_symmetry_2 3_545 _pdbx_validate_symm_contact.dist 2.16 # _pdbx_validate_rmsd_angle.id 1 _pdbx_validate_rmsd_angle.PDB_model_num 1 _pdbx_validate_rmsd_angle.auth_atom_id_1 O _pdbx_validate_rmsd_angle.auth_asym_id_1 A _pdbx_validate_rmsd_angle.auth_comp_id_1 ASN _pdbx_validate_rmsd_angle.auth_seq_id_1 25 _pdbx_validate_rmsd_angle.PDB_ins_code_1 ? _pdbx_validate_rmsd_angle.label_alt_id_1 ? _pdbx_validate_rmsd_angle.auth_atom_id_2 C _pdbx_validate_rmsd_angle.auth_asym_id_2 A _pdbx_validate_rmsd_angle.auth_comp_id_2 ASN _pdbx_validate_rmsd_angle.auth_seq_id_2 25 _pdbx_validate_rmsd_angle.PDB_ins_code_2 ? _pdbx_validate_rmsd_angle.label_alt_id_2 ? _pdbx_validate_rmsd_angle.auth_atom_id_3 N _pdbx_validate_rmsd_angle.auth_asym_id_3 A _pdbx_validate_rmsd_angle.auth_comp_id_3 GLU _pdbx_validate_rmsd_angle.auth_seq_id_3 26 _pdbx_validate_rmsd_angle.PDB_ins_code_3 ? _pdbx_validate_rmsd_angle.label_alt_id_3 ? _pdbx_validate_rmsd_angle.angle_value 112.16 _pdbx_validate_rmsd_angle.angle_target_value 122.70 _pdbx_validate_rmsd_angle.angle_deviation -10.54 _pdbx_validate_rmsd_angle.angle_standard_deviation 1.60 _pdbx_validate_rmsd_angle.linker_flag Y # loop_ _pdbx_validate_torsion.id _pdbx_validate_torsion.PDB_model_num _pdbx_validate_torsion.auth_comp_id _pdbx_validate_torsion.auth_asym_id _pdbx_validate_torsion.auth_seq_id _pdbx_validate_torsion.PDB_ins_code _pdbx_validate_torsion.label_alt_id _pdbx_validate_torsion.phi _pdbx_validate_torsion.psi 1 1 LYS A 14 ? ? -110.92 -154.29 2 1 ASN A 25 ? ? 84.37 -12.01 3 1 PRO A 142 ? ? -75.99 -164.62 4 1 LYS B 14 ? ? -113.47 -155.68 5 1 GLU B 23 ? ? -115.22 61.95 # loop_ _pdbx_distant_solvent_atoms.id _pdbx_distant_solvent_atoms.PDB_model_num _pdbx_distant_solvent_atoms.auth_atom_id _pdbx_distant_solvent_atoms.label_alt_id _pdbx_distant_solvent_atoms.auth_asym_id _pdbx_distant_solvent_atoms.auth_comp_id _pdbx_distant_solvent_atoms.auth_seq_id _pdbx_distant_solvent_atoms.PDB_ins_code _pdbx_distant_solvent_atoms.neighbor_macromolecule_distance _pdbx_distant_solvent_atoms.neighbor_ligand_distance 1 1 O ? A HOH 471 ? 6.79 . 2 1 O ? A HOH 472 ? 6.98 . 3 1 O ? B HOH 510 ? 5.90 . 4 1 O ? B HOH 511 ? 7.08 . # loop_ _pdbx_unobs_or_zero_occ_atoms.id _pdbx_unobs_or_zero_occ_atoms.PDB_model_num _pdbx_unobs_or_zero_occ_atoms.polymer_flag _pdbx_unobs_or_zero_occ_atoms.occupancy_flag _pdbx_unobs_or_zero_occ_atoms.auth_asym_id _pdbx_unobs_or_zero_occ_atoms.auth_comp_id _pdbx_unobs_or_zero_occ_atoms.auth_seq_id _pdbx_unobs_or_zero_occ_atoms.PDB_ins_code _pdbx_unobs_or_zero_occ_atoms.auth_atom_id _pdbx_unobs_or_zero_occ_atoms.label_alt_id _pdbx_unobs_or_zero_occ_atoms.label_asym_id _pdbx_unobs_or_zero_occ_atoms.label_comp_id _pdbx_unobs_or_zero_occ_atoms.label_seq_id _pdbx_unobs_or_zero_occ_atoms.label_atom_id 1 1 Y 1 A THR 130 ? OG1 ? A THR 131 OG1 2 1 Y 1 A THR 130 ? CG2 ? A THR 131 CG2 3 1 Y 1 B THR 130 ? OG1 ? B THR 131 OG1 4 1 Y 1 B THR 130 ? CG2 ? B THR 131 CG2 # loop_ _pdbx_unobs_or_zero_occ_residues.id _pdbx_unobs_or_zero_occ_residues.PDB_model_num _pdbx_unobs_or_zero_occ_residues.polymer_flag _pdbx_unobs_or_zero_occ_residues.occupancy_flag _pdbx_unobs_or_zero_occ_residues.auth_asym_id _pdbx_unobs_or_zero_occ_residues.auth_comp_id _pdbx_unobs_or_zero_occ_residues.auth_seq_id _pdbx_unobs_or_zero_occ_residues.PDB_ins_code _pdbx_unobs_or_zero_occ_residues.label_asym_id _pdbx_unobs_or_zero_occ_residues.label_comp_id _pdbx_unobs_or_zero_occ_residues.label_seq_id 1 1 Y 1 A HIS 209 ? A HIS 210 2 1 Y 1 A HIS 210 ? A HIS 211 # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 2 N-ACETYL-D-GLUCOSAMINE NAG 3 BETA-D-MANNOSE BMA 4 water HOH #